EC 7.1 Catalysing the translocation of hydrons
EC 7.2 Catalysing the translocation of inorganic cations
EC 7.3 Catalysing the translocation of inorganic anions and their chelates
EC 7.4 Catalysing the translocation of amino acids and peptides
EC 7.5 Catalysing the translocation of carbohydrates and their derivatives
EC 7.6 Catalysing the translocation of other compounds
EC 7.1.1 Hydron translocation or charge separation linked to oxidoreductase reactions
EC 7.1.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
EC 7.1.3 Hydron translocation or charge separation linked to oxidoreductase reactions
EC 7.1.1.1 proton-translocating NAD(P)+ transhydrogenase
EC 7.1.1.3 ubiquinol oxidase (H+-transporting)
EC 7.1.1.4 caldariellaquinol oxidase (H+-transporting)
EC 7.1.1.5 menaquinol oxidase (H+-transporting)
EC 7.1.1.6 plastoquinol—plastocyanin reductase
EC 7.1.1.7 quinol—cytochrome-c reductase
EC 7.1.1.9 cytochrome-c oxidase
EC 7.1.1.10 ferredoxin—quinone oxidoreductase (H+-translocating)
EC 7.1.1.11 ferredoxin—NAD+ oxidoreductase (H+-transporting)
EC 7.1.1.12 succinate dehydrogenase (electrogenic, proton-motive force generating)
Accepted name: proton-translocating NAD(P)+ transhydrogenase
Reaction: NADPH + NAD+ + H+[side 1] = NADP+ + NADH + H+[side 2]
Other name(s): pntA (gene name); pntB (gene name); NNT (gene name)
Systematic name: NADPH:NAD+ oxidoreductase (H+-transporting)
Comments: The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Clarke, D.M. and Bragg, P.D. Cloning and expression of the transhydrogenase gene of Escherichia coli. J. Bacteriol. 162 (1985) 367-373. [PMID: 3884596]
2. Clarke, D.M. and Bragg, P.D. Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 149 (1985) 517-523. [PMID: 3891338]
3. Glavas, N.A., Hou, C. and Bragg, P.D. Involvement of histidine-91 of the β subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochemistry 34 (1995) 7694-7702. [PMID: 7779816]
4. Sauer, U., Canonaco, F., Heri, S., Perrenoud, A. and Fischer, E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279 (2004) 6613-6619. [PMID: 14660605]
5. Bizouarn, T., Fjellstrom, O., Meuller, J., Axelsson, M., Bergkvist, A., Johansson, C., Goran Karlsson, B. and Rydstrom, J. Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties. Biochim. Biophys. Acta 1457 (2000) 211-228. [PMID: 10773166]
6. White, S.A., Peake, S.J., McSweeney, S., Leonard, G., Cotton, N.P. and Jackson, J.B. The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria. Structure 8 (2000) 1-12. [PMID: 10673423]
7. Johansson, T., Oswald, C., Pedersen, A., Tornroth, S., Okvist, M., Karlsson, B.G., Rydstrom, J. and Krengel, U. X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli. J. Mol. Biol. 352 (2005) 299-312. [PMID: 16083909]
8. Meimaridou, E., Kowalczyk, J., Guasti, L., Hughes, C.R., Wagner, F., Frommolt, P., Nurnberg, P., Mann, N.P., Banerjee, R., Saka, H.N., Chapple, J.P., King, P.J., Clark, A.J. and Metherell, L.A. Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency. Nat. Genet. 44 (2012) 740-742. [PMID: 22634753]
Accepted name: NADH:ubiquinone reductase (H+-translocating)
Reaction: NADH + H+ + an ubiquinone + 4 H+[side 1] = NAD+ + an ubiquinol + 4 H+[side 2]
Other name(s): ubiquinone reductase (ambiguous); type 1 dehydrogenase; complex 1 dehydrogenase; coenzyme Q reductase (ambiguous); complex I (electron transport chain); complex I (mitochondrial electron transport); complex I (NADH:Q1 oxidoreductase); dihydronicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous); DPNH-coenzyme Q reductase (ambiguous); DPNH-ubiquinone reductase (ambiguous); mitochondrial electron transport complex 1; mitochondrial electron transport complex I; NADH coenzyme Q1 reductase; NADH-coenzyme Q oxidoreductase (ambiguous); NADH-coenzyme Q reductase (ambiguous); NADH-CoQ oxidoreductase (ambiguous); NADH-dehydrogenase (ubiquinone) (ambiguous); NADH-CoQ reductase (ambiguous); NADH-ubiquinone reductase (ambiguous); NADH-ubiquinone oxidoreductase (ambiguous); NADH-ubiquinone-1 reductase; reduced nicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous); NADH:ubiquinone oxidoreductase complex; NADH-Q6 oxidoreductase (ambiguous); electron transfer complex I; NADH2 dehydrogenase (ubiquinone)
Systematic name: NADH:ubiquinone oxidoreductase
Comments: The enzyme is a very large complex that participates in electron transfer chains of mitochondria and aerobic bacteria, transferring two electrons from NADH to a ubiquinone in the membrane's ubiquinone pool while pumping additional protons across the membrane, generating proton motive force. Different reports disagree whether the enzyme pumps 3 or 4 protons. Reversed electron transport through this enzyme can reduce NAD+ to NADH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-04-0
References:
1. Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd edn, vol. 4, Plenum Press, New York, 1985, pp. 1-70.
2. Herter, S.M., Kortluke, C.M. and Drews, G. Complex I of Rhodobacter capsulatus and its role in reverted electron transport. Arch. Microbiol. 169 (1998) 98-105. [PMID: 9446680]
3. Hunte, C., Zickermann, V. and Brandt, U. Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329 (2010) 448-451. [PMID: 20595580]
4. Efremov, R.G., Baradaran, R. and Sazanov, L.A. The architecture of respiratory complex I. Nature 465 (2010) 441-445. [PMID: 20505720]
5. Wikstrom, M. and Hummer, G. Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications. Proc. Natl. Acad. Sci. USA 109 (2012) 4431-4436. [PMID: 22392981]
Accepted name: ubiquinol oxidase (H+-transporting)
Reaction: 2 quinol + O2[side 2] + 8 H+[side 2] = 2 quinone + 2 H2O[side 2] + 8 H+[side 1]
Other name(s): cyoABCD (gene names); cytochrome bo3 oxidase; cytochrome bb3 oxidase; cytochrome bo oxidase; Cyo oxidase; ubiquinol:O2 oxidoreductase (H+-transporting); ubiquinol:oxygen oxidoreductase (H+-transporting)
Systematic name: quinol:oxygen oxidoreductase (H+-transporting)
Comments: Contains a dinuclear centre comprising heme and copper. This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) of enzymes that have been characterized so far is 2. cf. EC 7.1.1.7, ubiquinol oxidase ubiquinol oxidase (electrogenic, proton-motive force generating).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Miyoshi-Akiyama, T., Hayashi, M. and Unemoto, T. Purification and properties of cytochrome bo-type ubiquinol oxidase from a marine bacterium Vibrio alginolyticus. Biochim. Biophys Acta 1141 (1993) 283-287. [PMID: 8443214]
2. de Gier, J.W., Lubben, M., Reijnders, W.N., Tipker, C.A., Slotboom, D.J., van Spanning, R.J., Stouthamer, A.H. and van der Oost, J. The terminal oxidases of Paracoccus denitrificans. Mol. Microbiol. 13 (1994) 183-196. [PMID: 7984100]
3. Howitt, C.A. and Vermaas, W.F. Quinol and cytochrome oxidases in the cyanobacterium Synechocystis sp. PCC 6803. Biochemistry 37 (1998) 17944-17951. [PMID: 9922162]
4. Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S. and Wikstrom, M. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat. Struct. Biol. 7 (2000) 910-917. [PMID: 11017202]
5. Morales, G., Ugidos, A. and Rojo, F. Inactivation of the Pseudomonas putida cytochrome o ubiquinol oxidase leads to a significant change in the transcriptome and to increased expression of the CIO and cbb3-1 terminal oxidases. Environ. Microbiol. 8 (2006) 1764-1774. [PMID: 16958757]
6. Stenberg, F., von Heijne, G. and Daley, D.O. Assembly of the cytochrome bo3 complex. J. Mol. Biol. 371 (2007) 765-773. [PMID: 17583738]
7. Yap, L.L., Lin, M.T., Ouyang, H., Samoilova, R.I., Dikanov, S.A. and Gennis, R.B. The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli. Biochim. Biophys. Acta 1797 (2010) 1924-1932. [PMID: 20416270]
8. Choi, S.K., Lin, M.T., Ouyang, H. and Gennis, R.B. Searching for the low affinity ubiquinone binding site in cytochrome bo3 from Escherichia coli. Biochim Biophys Acta Bioenerg 1858 (2017) 366-370. [PMID: 28235459]
9. Choi, S.K., Schurig-Briccio, L., Ding, Z., Hong, S., Sun, C. and Gennis, R.B. Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli. J. Am. Chem. Soc. 139 (2017) 8346-8354. [PMID: 28538096]
10. Graf, S., Brzezinski, P. and von Ballmoos, C. The proton pumping bo oxidase from Vitreoscilla. Sci. Rep. 9 (2019) 4766. [PMID: 30886219]
Accepted name: caldariellaquinol oxidase (H+-transporting)
Reaction: 2 caldariellaquinol + O2 + n H+[side 1] = 2 caldariellaquinone + 2 H2O + n H+[side 2]
Glossary: caldariellaquinol = 6-(3,7,11,15,19,23-hexamethyltetracosyl)-5-(methylsulfanyl)-1-benzothiophene-4,7-diol
Other name(s): SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa3-type quinol oxidase; aa3 quinol oxidase; cytochrome aa3; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa3-type oxidase; caldariellaquinol:O2 oxidoreductase (H+-transporting)
Systematic name: caldariellaquinol:oxygen oxidoreductase (H+-transporting)
Comments: A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Gleissner, M., Kaiser, U., Antonopoulos, E. and Schafer, G. The archaeal SoxABCD complex is a proton pump in Sulfolobus acidocaldarius. J. Biol. Chem. 272 (1997) 8417-8426. [PMID: 9079667]
2. Purschke, W.G., Schmidt, C.L., Petersen, A. and Schafer, G. The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization. J. Bacteriol. 179 (1997) 1344-1353. [PMID: 9023221]
3. Gilderson, G., Aagaard, A., Gomes, C.M., Adelroth, P., Teixeira, M. and Brzezinski, P. Kinetics of electron and proton transfer during O2 reduction in cytochrome aa3 from A. ambivalens: an enzyme lacking Glu(I-286). Biochim. Biophys. Acta 1503 (2001) 261-270. [PMID: 11115638]
4. Komorowski, L., Verheyen, W. and Schafer, G. The archaeal respiratory supercomplex SoxM from S. acidocaldarius combines features of quinole and cytochrome c oxidases. Biol. Chem. 383 (2002) 1791-1799. [PMID: 12530544]
5. Muller, F.H., Bandeiras, T.M., Urich, T., Teixeira, M., Gomes, C.M. and Kletzin, A. Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase. Mol. Microbiol. 53 (2004) 1147-1160. [PMID: 15306018]
6. Bandeiras, T.M., Pereira, M.M., Teixeira, M., Moenne-Loccoz, P. and Blackburn, N.J. Structure and coordination of CuB in the Acidianus ambivalens aa3 quinol oxidase heme-copper center. J. Biol. Inorg. Chem. 10 (2005) 625-635. [PMID: 16163550]
Accepted name: menaquinol oxidase (H+-transporting)
Reaction: 2 menaquinol + O2 + n H+[side 1] = 2 menaquinone + 2 H2O + n H+[side 2]
Other name(s): cytochrome aa3-600 oxidase; cytochrome bd oxidase; menaquinol:O2 oxidoreductase (H+-transporting)
Systematic name: menaquinol:oxygen oxidoreductase (H+-transporting)
Comments: Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.The enzyme also pumps protons across the membrane bilayer, generating a proton motive force.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Lauraeus, M. and Wikstrom, M. The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties. J. Biol. Chem. 268 (1993) 11470-11473. [PMID: 8388393]
2. Lemma, E., Simon, J., Schagger, H. and Kroger, A. Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis. Arch. Microbiol. 163 (1995) 432-438. [PMID: 7575098]
3. Yi, S.M., Narasimhulu, K.V., Samoilova, R.I., Gennis, R.B. and Dikanov, S.A. Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis. J. Biol. Chem. 285 (2010) 18241-18251. [PMID: 20351111]
Accepted name: plastoquinol—plastocyanin reductase
Reaction: plastoquinol + 2 oxidized plastocyanin + 2 H+[side 1] = plastoquinone + 2 reduced plastocyanin + 4 H+[side 2]
Other name(s): plastoquinol/plastocyanin oxidoreductase; cytochrome f/b6 complex; cytochrome b6f complex
Systematic name: plastoquinol:oxidized-plastocyanin oxidoreductase
Comments: Contains two b-type cytochromes, two c-type cytochromes (cn and f), and a [2Fe-2S] Rieske cluster. The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. In chloroplasts, protons are translocated through the thylakoid membrane from the stroma to the lumen. The mechanism occurs through the Q cycle as in EC 7.1.1.8, quinol—cytochrome-c reductase (complex III) and involves electron bifurcation.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hurt, E. and Hauska, G. A cytochrome f/b6 complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts. Eur. J. Biochem. 117 (1981) 591-595. [PMID: 6269845]
2. Cramer, W.A. and Zhang, H. Consequences of the structure of the cytochrome b6f complex for its charge transfer pathways. Biochim. Biophys. Acta 1757 (2006) 339-345. [PMID: 16787635]
Accepted name: quinol oxidase (electrogenic, proton-motive force generating)
Reaction: 2 quinol + O2[side 2] + 4 H+[side 2] = 2 quinone + 2 H2O[side 2] + 4 H+[side 1] (overall reaction)
(1a) 2 quinol = 2 quinone + 4 H+[side 1] + 4 e-
(1b) O2[side 2] + 4 H+[side 2] + 4 e- = 2 H2O[side 2]
Other name(s): cydAB (gene names); appBC (gene names); cytochrome bd oxidase; cytochrome bd-I oxidase; cytochrome bd-II oxidase; ubiquinol:O2 oxidoreductase (electrogenic, non H+-transporting); ubiquinol oxidase (electrogenic, proton-motive force generating); ubiquinol oxidase (electrogenic, non H+-transporting)
Systematic name: quinol:oxygen oxidoreductase (electrogenic, non H+-transporting)
Comments: This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. cf. EC 7.1.1.3, ubiquinol oxidase (H+-transporting).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Miller, M.J., Hermodson, M. and Gennis, R.B. The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits. J. Biol. Chem. 263 (1988) 5235-5240. [PMID: 3281937]
2. Puustinen, A., Finel, M., Haltia, T., Gennis, R.B. and Wikstrom, M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry 30 (1991) 3936-3942. [PMID: 1850294]
3. Belevich, I., Borisov, V.B., Zhang, J., Yang, K., Konstantinov, A.A., Gennis, R.B. and Verkhovsky, M.I. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Proc. Natl. Acad. Sci. USA 102 (2005) 3657-3662. [PMID: 15728392]
4. Lenn, T., Leake, M.C. and Mullineaux, C.W. Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo. Mol. Microbiol. 70 (2008) 1397-1407. [PMID: 19019148]
5. Shepherd, M., Sanguinetti, G., Cook, G.M. and Poole, R.K. Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism. J. Biol. Chem. 285 (2010) 18464-18472. [PMID: 20392690]
6. Borisov, V.B., Murali, R., Verkhovskaya, M.L., Bloch, D.A., Han, H., Gennis, R.B. and Verkhovsky, M.I. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc. Natl. Acad. Sci. USA 108 (2011) 17320-17324. [PMID: 21987791]
7. Borisov, V.B., Gennis, R.B., Hemp, J. and Verkhovsky, M.I. The cytochrome bd respiratory oxygen reductases. Biochim. Biophys. Acta 1807 (2011) 1398-1413. [PMID: 21756872]
Accepted name: quinol—cytochrome-c reductase
Reaction: quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2]
Other name(s): ubiquinol—cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitochondrial electron transport); ubiquinone-cytochrome c reductase; ubiquinol-cytochrome c oxidoreductase; reduced coenzyme Q-cytochrome c reductase; ubiquinone-cytochrome c oxidoreductase; reduced ubiquinone-cytochrome c oxidoreductase; mitochondrial electron transport complex III; ubiquinol-cytochrome c-2 oxidoreductase; ubiquinone-cytochrome b-c1 oxidoreductase; ubiquinol-cytochrome c2 reductase; ubiquinol-cytochrome c1 oxidoreductase; CoQH2-cytochrome c oxidoreductase; ubihydroquinol:cytochrome c oxidoreductase; coenzyme QH2-cytochrome c reductase; QH2:cytochrome c oxidoreductase; ubiquinol:ferricytochrome-c oxidoreductase
Systematic name: quinol:ferricytochrome-c oxidoreductase
Comments: The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3, NADH dehydrogenase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Marres, C.A.M. and Slater, E.C. Polypeptide composition of purified QH2:cytochrome c oxidoreductase from beef-heart mitochondria. Biochim. Biophys. Acta 462 (1977) 531-548. [PMID: 597492]
2. Rieske, J.S. Composition, structure, and function of complex III of the respiratory chain. Biochim. Biophys. Acta 456 (1976) 195-247. [PMID: 788795]
3. Wikström, M., Krab, K. and Saraste, M. Proton-translocating cytochrome complexes. Annu. Rev. Biochem. 50 (1981) 623-655. [PMID: 6267990]
4. Sone, N., Tsuchiya, N., Inoue, M. and Noguchi, S. Bacillus stearothermophilus qcr operon encoding rieske FeS protein, cytochrome b6, and a novel-type cytochrome c1 of quinol-cytochrome c reductase. J. Biol. Chem. 271 (1996) 12457-12462. [PMID: 8647852]
5. Yu, J. and Le Brun, N.E. Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. J. Biol. Chem. 273 (1998) 8860-8866. [PMID: 9535866]
6. Elbehti, A., Nitschke, W., Tron, P., Michel, C. and Lemesle-Meunier, D. Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc1-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans. J. Biol. Chem. 274 (1999) 16760-16765. [PMID: 10358017]
Accepted name: cytochrome-c oxidase
Reaction: 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4 H+[side 2]
For diagram of reaction click here.
Other name(s): cytochrome aa3; cytochrome caa3; cytochrome bb3; cytochrome cbb3; cytochrome ba3; cytochrome a3; Warburg's respiratory enzyme; indophenol oxidase; indophenolase; complex IV (mitochondrial electron transport); ferrocytochrome c oxidase; cytochrome oxidase (ambiguous); NADH cytochrome c oxidase (incorrect)
Systematic name: ferrocytochrome-c:oxygen oxidoreductase
Comments: An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms. The reduction of O2 to water is accompanied by the extrusion of four protons. The cytochrome-aa3 enzymes of mitochondria and many bacterial species are the most abundant group, but other variations, such as the bacterial cytochrome-cbb3 enzymes, also exist. All of the variants have a conserved catalytic core subunit (subunit I) that contains a low-spin heme (of a- or b-type), a binuclear metal centre composed of a high-spin heme iron (of a-, o-, or b-type heme, referred to as a3, o3 or b3 heme), and a Cu atom (CuB). Besides subunit I, the enzyme usually has at least two other core subunits: subunit II is the primary electron acceptor; subunit III usually does not contain any cofactors, but in the case of cbb3-type enzymes it is a diheme c-type cytochrome. While most bacterial enzymes consist of only 3-4 subunits, the mitochondrial enzyme is much more complex and contains 14 subunits.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-16-5
References:
1. Keilin, D. and Hartree, E.F. Cytochrome oxidase. Proc. R. Soc. Lond. B Biol. Sci. 125 (1938) 171-186.
2. Keilin, D. and Hartree, E.F. Cytochrome and cytochrome oxidase. Proc. R. Soc. Lond. B Biol. Sci. 127 (1939) 167-191.
3. Wainio, W.W., Eichel, B. and Gould, A. Ion and pH optimum for the oxidation of ferrocytochrome c by cytochrome c oxidase in air. J. Biol. Chem. 235 (1960) 1521-1525.
4. Yonetani, T. Studies on cytochrome oxidase. II. Steady state properties. J. Biol. Chem. 235 (1960) 3138-3243. [PMID: 13787372]
5. Yonetani, T. Studies on cytochrome oxidase. III. Improved purification and some properties. J. Biol. Chem. 236 (1961) 1680-1688. [PMID: 13787373]
6. Henning, W., Vo, L., Albanese, J. and Hill, B.C. High-yield purification of cytochrome aa3 and cytochrome caa3 oxidases from Bacillus subtilis plasma membranes. Biochem. J. 309 (1995) 279-283. [PMID: 7619069]
7. Keightley, J.A., Zimmermann, B.H., Mather, M.W., Springer, P., Pastuszyn, A., Lawrence, D.M. and Fee, J.A. Molecular genetic and protein chemical characterization of the cytochrome ba3 from Thermus thermophilus HB8. J. Biol. Chem. 270 (1995) 20345-20358. [PMID: 7657607]
8. Ducluzeau, A.L., Ouchane, S. and Nitschke, W. The cbb3 oxidases are an ancient innovation of the domain bacteria. Mol. Biol. Evol. 25 (2008) 1158-1166. [PMID: 18353797]
Accepted name: ferredoxin—quinone oxidoreductase (H+-translocating)
Reaction: 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
Other name(s): NDH-1L complex; NDH-1L' complex; NDH11 complex; NDH12 complex
Systematic name: ferredoxin:quinone oxidoreductase (H+-translocating)
Comments: The enzyme, present in plants and cyanobacteria, couples electron transport from ferredoxin to plastoquinone and proton pumping from the cytoplasm to the thylakoid lumen. It participates in cyclic electron flow, retuning electrons generated by photosystem I to the plastoquinone pool, thus bypassing the generation of reducing power. It may also participate in respiration using electrons originating from NADPH via the action of EC 1.18.1.2, ferredoxin—NADP+ reductase (FNR) operating in the direction of ferredoxin reduction. It is a large complex, with some of its subunits resembling those from the bacterial/mitochondrial EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating). However, it lacks the NADH-oxidizing module and instead has a module that interacts with ferredoxin. Several forms of the enzyme exist, differing in their exact combination of subunits used. Some of the forms participate in carbon dioxide hydration rather than electron transfer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Arteni, A.A., Zhang, P., Battchikova, N., Ogawa, T., Aro, E.M. and Boekema, E.J. Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy. Biochim. Biophys. Acta 1757 (2006) 1469-1475. [PMID: 16844076]
2. Battchikova, N., Wei, L., Du, L., Bersanini, L., Aro, E.M. and Ma, W. Identification of novel Ssl0352 protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH:plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803. J. Biol. Chem. 286 (2011) 36992-37001. [PMID: 21880717]
3. Yamamoto, H. and Shikanai, T. In planta mutagenesis of Src homology 3 domain-like fold of NdhS, a ferredoxin-binding subunit of the chloroplast NADH dehydrogenase-like complex in Arabidopsis: a conserved Arg-193 plays a critical role in ferredoxin binding. J. Biol. Chem. 288 (2013) 36328-36337. [PMID: 24225949]
4. Ma, W. and Ogawa, T. Oxygenic photosynthesis-specific subunits of cyanobacterial NADPH dehydrogenases. IUBMB Life 67 (2015) 3-8. [PMID: 25564967]
5. Peltier, G., Aro, E.M. and Shikanai, T. NDH-1 and NDH-2 plastoquinone reductases in oxygenic photosynthesis. Annu. Rev. Plant Biol. 67 (2016) 55-80. [PMID: 26735062]
6. Laughlin, T.G., Bayne, A.N., Trempe, J.F., Savage, D.F. and Davies, K.M. Structure of the complex I-like molecule NDH of oxygenic photosynthesis. Nature 566 (2019) 411-414. [PMID: 30742075]
7. Schuller, J.M., Birrell, J.A., Tanaka, H., Konuma, T., Wulfhorst, H., Cox, N., Schuller, S.K., Thiemann, J., Lubitz, W., Setif, P., Ikegami, T., Engel, B.D., Kurisu, G. and Nowaczyk, M.M. Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science 363 (2019) 257-260. [PMID: 30573545]
8. Zhang, C., Shuai, J., Ran, Z., Zhao, J., Wu, Z., Liao, R., Wu, J., Ma, W. and Lei, M. Structural insights into NDH-1 mediated cyclic electron transfer. Nat. Commun. 11 (2020) 888. [PMID: 32060291]
Accepted name: ferredoxin—NAD+ oxidoreductase (H+-transporting)
Reaction: 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + 2 H+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + 2 H+[side 2]
Other name(s): Rnf complex (ambiguous); H+-translocating ferredoxin:NAD+ oxidoreductase
Systematic name: ferredoxin:NAD+ oxidoreductase (H+-transporting)
Comments: This iron-sulfur and flavin-containing electron transport complex, isolated from some anaerobic bacteria, couples the energy from reduction of NAD+ by ferredoxin to pumping protons out of the cell, generating a proton motive force across the cytoplasmic membrane. Most similar complexes pump sodium ions rather than protons [cf. EC 7.2.1.2, ferredoxin—NAD+ oxidoreductase (Na+-transporting)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Tremblay, P.L., Zhang, T., Dar, S.A., Leang, C. and Lovley, D.R. The Rnf complex of Clostridium ljungdahlii is a proton-translocating ferredoxin:NAD+ oxidoreductase essential for autotrophic growth. mBio 4 (2012) e00406. [PMID: 23269825]
2. Wang, L., Bradstock, P., Li, C., McInerney, M.J. and Krumholz, L.R. The role of Rnf in ion gradient formation in Desulfovibrio alaskensis. PeerJ 4 (2016) e1919. [PMID: 27114876]
Accepted name: succinate dehydrogenase (electrogenic, proton-motive force generating)
Reaction: succinate + menaquinone + 2 H+[side 1] = fumarate + menaquinol + 2 H+[side 2]
Systematic name: succinate:quinone oxidoreductase (electrogenic, proton-motive force generating)
Comments: The enzyme is very similar to EC 1.3.5.1, succinate dehydrogenase, but differs by containing two heme molecules (located in the membrane anchor component) in addition to FAD and three iron-sulfur clusters. Unlike EC 1.3.5.1, this enzyme catalyses an electrogenic reaction, enabled by electron-bifurcation via the heme molecules. In the direction of succinate oxidation by menaquinone, which is endergonic, the reaction is driven by the transmembrane electrochemical proton potential. In the direction of fumarate reduction, the electrogenic electron transfer reaction is compensated by transmembrane proton transfer pathway known as the E-pathway, which results in overall electroneutrality.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lancaster, C.R. Wolinella succinogenes quinol:fumarate reductase-2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer. Biochim. Biophys. Acta 1565 (2002) 215-231. [PMID: 12409197]
2. Madej, M.G., Nasiri, H.R., Hilgendorff, N.S., Schwalbe, H., Unden, G. and Lancaster, C.R. Experimental evidence for proton motive force-dependent catalysis by the diheme-containing succinate:menaquinone oxidoreductase from the Gram-positive bacterium Bacillus licheniformis. Biochemistry 45 (2006) 15049-15055. [PMID: 17154542]
3. Lancaster, C.R., Herzog, E., Juhnke, H.D., Madej, M.G., Muller, F.G., Paul, R. and Schleidt, P.G. Electroneutral and electrogenic catalysis by dihaem-containing succinate:quinone oxidoreductases. Biochem Soc Trans. 36 (2008) 996-1000. [PMID: 18793177]
4. Lancaster, C.R. The di-heme family of respiratory complex II enzymes. Biochim. Biophys. Acta 1827 (2013) 679-687. [PMID: 23466335]
5. Guan, H.H., Hsieh, Y.C., Lin, P.J., Huang, Y.C., Yoshimura, M., Chen, L.Y., Chen, S.K., Chuankhayan, P., Lin, C.C., Chen, N.C., Nakagawa, A., Chan, S.I. and Chen, C.J. Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas. Sci. Rep. 8 (2018) 14935. [PMID: 30297797]
Contents
EC 7.1.2.1 H+-exporting ATPase
EC 7.1.2.2 H+-transporting two-sector ATPase
Accepted name: H+-exporting ATPase
Reaction: ATP + H2O + H+[side 1] = ADP + phosphate + H+[side 2]
Other name(s): proton-translocating ATPase; yeast plasma membrane H+-ATPase; yeast plasma membrane ATPase; ATP phosphohydrolase (ambiguous)
Systematic name: ATP phosphohydrolase (H+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Goffeau, A. and Slayman, C. The proton-translocating ATPase of the fungal plasma membrane. Biochim. Biophys. Acta 639 (1981) 197-223. [PMID: 6461354]
2. Serrano, R., Kielland-Brandt, M.C. and Fink, G.R. Yeast plasma membrane ATPase is essential for growth and has homology with (Na++K+)-, K+-and Ca2+-ATPases. Nature 319 (1986) 689-693. [PMID: 3005867]
3. Serrano, R. and Portillo, F. Catalytic and regulatory sites of yeast plasma membrane H+-ATPase studied by directed mutagenesis. Biochim. Biophys. Acta 1018 (1990) 195-199. [PMID: 2144186]
4. Perlin, D.S., San Francisco, M.J., Slayman, C.W. and Rosen, B.P. H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli. Arch. Biochem. Biophys. 248 (1986) 53-61. [PMID: 2425739]
Accepted name: H+-transporting two-sector ATPase
Reaction: ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
Glossary: In Fo, the "o" refers to oligomycin. F0 is incorrect
Other name(s): ATP synthase; F1-ATPase; FoF1-ATPase; H+-transporting ATPase; mitochondrial ATPase; coupling factors (F0, F1 and CF1); chloroplast ATPase; bacterial Ca2+/Mg2+ ATPase
Systematic name: ATP phosphohydrolase (H+-transporting)
Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 α- and 3 β-subunits) is connected via the δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9-12 c subunits rotate by consecutive 120° angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Perlin, D.S., San Francisco, M.J., Slayman, C.W. and Rosen, B.P. H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli. Arch. Biochem. Biophys. 248 (1986) 53-61. [PMID: 2425739]
2. Boyer, P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215-250. [PMID: 8417777]
3. Abrahams, J.P., Leslie, A.G.W., Lutter, R. and Walker, J.F. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 375 (1994) 621-628. [PMID: 8065448]
4. Blair, A., Ngo, L., Park, J., Paulsen, I.T. and Saier, M.H., Jr. Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the FoF1-ATPases of bacteria, chloroplasts and mitochondria. Microbiology 142 (1996) 17-32. [PMID: 8581162]
5. Noji, H., Yasuda, R., Yoshida, M. and Kinosita, K., Jr. Direct observation of the rotation of F1-ATPase. Nature 386 (1997) 299-302. [PMID: 9069291]
6. Turina, P., Samoray, D. and Graber, P. H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes. EMBO J. 22 (2003) 418-426. [PMID: 12554643]
Contents
EC 7.1.3.1 H+-exporting diphosphatase
EC 7.1.3.2 transferred now EC 7.2.3.1
Accepted name: H+-exporting diphosphatase
Reaction: diphosphate + H2O + H+[side 1] = 2 phosphate + H+[side 2]
Other name(s): H+-PPase; proton-pumping pyrophosphatase; vacuolar H+-pyrophosphatase; hydrogen-translocating pyrophosphatase; proton-pumping dihosphatase
Systematic name: diphosphate phosphohydrolase (H+-transporting)
Comments: This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Rea, P.A. and Poole, R.J. Chromatographic resolution of H+-translocating pyrophosphatase from H+-translocating ATPase of higher plant tonoplast. Plant Physiol. 81 (1986) 126-129. [PMID: 16664761]
2. Sarafian, V. and Poole, R.J. Purification of an H+-translocating inorganic pyrophosphatase from vacuole membranes of red beet. Plant Physiol. 91 (1989) 34-38. [PMID: 16667022]
3. Hedrich, R., Kurkdjian, A., Guern, J. and Flugge, U.I. Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment. EMBO J. 8 (1989) 2835-2841. [PMID: 2479537]
4. Segami, S., Tomoyama, T., Sakamoto, S., Gunji, S., Fukuda, M., Kinoshita, S., Mitsuda, N., Ferjani, A. and Maeshima, M. Vacuolar H+-pyrophosphatase and cytosolic soluble pyrophosphatases cooperatively regulate pyrophosphate levels in Arabidopsis thaliana, Plant Cell 30 (2018) 1040-1061. [PMID: 29691313]
[EC 7.1.3.2 Transferred entry: now EC 7.2.3.1, Na+-exporting diphosphatase (EC 7.1.3.2 created 2021, deleted 2022)]
Accepted name: Na+-exporting diphosphatase
Reaction: diphosphate + H2O + Na+[side 1] = 2 phosphate + Na+[side 2]
Other name(s): Na+-translocating membrane pyrophosphatase; sodium-translocating pyrophosphatase
Systematic name: diphosphate phosphohydrolase (Na+-transporting)
Comments: Requires Na+ and K+. This enzyme, found in some bacteria and archaea, couples the energy from diphosphate hydrolysis to active sodium translocation across the membrane. The enzyme is electrogenic, as the Na+ transport results in generation of a positive potential in the inner side of the membrane.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Belogurov, G.A., Malinen, A.M., Turkina, M.V., Jalonen, U., Rytkonen, K., Baykov, A.A. and Lahti, R. Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium for activity. Biochemistry 44 (2005) 2088-2096. [PMID: 15697234]
2. Malinen, A.M., Belogurov, G.A., Baykov, A.A. and Lahti, R. Na+-pyrophosphatase: a novel primary sodium pump. Biochemistry 46 (2007) 8872-8878. [PMID: 17605473]
3. Luoto, H.H., Belogurov, G.A., Baykov, A.A., Lahti, R. and Malinen, A.M. Na+-translocating membrane pyrophosphatases are widespread in the microbial world and evolutionarily precede H+-translocating pyrophosphatases. J. Biol. Chem. 286 (2011) 21633-21642. [PMID: 21527638]
EC 7.2.1 Linked to oxidoreductase reactions
EC 7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.2.4 Linked to decarboxylation
Contents
EC 7.2.1.1 NADH:ubiquinone reductase (Na+-transporting)
EC 7.2.1.2 ferredoxin—NAD+ oxidoreductase (Na+-transporting)
EC 7.2.1.3 ascorbate ferrireductase (transmembrane)
EC 7.2.1.4 tetrahydromethanopterin S-methyltransferase
Accepted name: NADH:ubiquinone reductase (Na+-transporting)
Reaction: NADH + H+ + ubiquinone + n Na+[side 1] = NAD+ + ubiquinol + n Na+[side 2]
Other name(s): Na+-translocating NADH-quinone reductase; (Na+-NQR)
Systematic name: NADH:ubiquinone oxidoreductase (Na+-translocating)
Comments: An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Beattie, P., Tan, K., Bourne, R.M., Leach, D., Rich, P.R. and Ward, F.B. Cloning and sequencing of four structural genes for the Na+-translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus. FEBS Lett. 356 (1994) 333-338. [PMID: 7805867]
2. Nakayama, Y., Hayashi, M. and Unemoto, T. Identification of six subunits constituting Na+-translocating NADH-quinone reductase from the marine Vibrio alginolyticus. FEBS Lett. 422 (1998) 240-242. [PMID: 9490015]
3. Bogachev, A.V., Bertsova, Y.V., Barquera, B. and Verkhovsky, M.I. Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi. Biochemistry 40 (2001) 7318-7323. [PMID: 11401580]
4. Barquera, B., Hellwig, P., Zhou, W., Morgan, J.E., Hase, C.C., Gosink, K.K., Nilges, M., Bruesehoff, P.J., Roth, A., Lancaster, C.R. and Gennis, R.B. Purification and characterization of the recombinant Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Biochemistry 41 (2002) 3781-3789. [PMID: 11888296]
5. Barquera, B., Nilges, M.J., Morgan, J.E., Ramirez-Silva, L., Zhou, W. and Gennis, R.B. Mutagenesis study of the 2Fe-2S center and the FAD binding site of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. Biochemistry 43 (2004) 12322-12330. [PMID: 15379571]
Accepted name: ferredoxin—NAD+ oxidoreductase (Na+-transporting)
Reaction: 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
Other name(s): Rnf complex (ambiguous); Na+-translocating ferredoxin:NAD+ oxidoreductase
Systematic name: ferredoxin:NAD+ oxidoreductase (Na+-transporting)
Comments: This iron-sulfur and flavin-containing electron transport complex, isolated from the bacterium Acetobacterium woodii, couples the energy from reduction of NAD+ by ferredoxin to pumping sodium ions out of the cell, generating a gradient across the cytoplasmic membrane.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Biegel, E., Schmidt, S. and Muller, V. Genetic, immunological and biochemical evidence for a Rnf complex in the acetogen Acetobacterium woodii. Environ Microbiol 11 (2009) 1438-1443. [PMID: 19222539]
2. Biegel, E. and Muller, V. Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase. Proc. Natl. Acad. Sci. USA 107 (2010) 18138-18142. [PMID: 20921383]
3. Hess, V., Schuchmann, K. and Muller, V. The ferredoxin:NAD+ oxidoreductase (Rnf) from the acetogen Acetobacterium woodii requires Na+ and is reversibly coupled to the membrane potential. J. Biol. Chem. 288 (2013) 31496-31502. [PMID: 24045950]
Accepted name: ascorbate ferrireductase (transmembrane)
Reaction: ascorbate[side 1] + Fe(III)[side 2] = monodehydroascorbate[side 1] + Fe(II)[side 2]
Other name(s): cytochrome b561 (ambiguous)
Systematic name: Fe(III):ascorbate oxidorectuctase (electron-translocating)
Comments: A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole. Acts on hexacyanoferrate(III) and other ferric chelates.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Flatmark, T. and Terland, O. Cytochrome b561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome. Biochim. Biophys. Acta 253 (1971) 487-491. [PMID: 4332308]
2. McKie, A.T., Barrow, D., Latunde-Dada, G.O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., Peters, T.J., Raja, K.B., Shirali, S., Hediger, M.A., Farzaneh, F. and Simpson, R.J. An iron-regulated ferric reductase associated with the absorption of dietary iron. Science 291 (2001) 1755-1759. [PMID: 11230685]
3. Su, D. and Asard, H. Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases. FEBS J. 273 (2006) 3722-3734. [PMID: 16911521]
4. Berczi, A., Su, D. and Asard, H. An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability. FEBS Lett. 581 (2007) 1505-1508. [PMID: 17376442]
5. Wyman, S., Simpson, R.J., McKie, A.T. and Sharp, P.A. Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro. FEBS Lett. 582 (2008) 1901-1906. [PMID: 18498772]
6. Glanfield, A., McManus, D.P., Smyth, D.J., Lovas, E.M., Loukas, A., Gobert, G.N. and Jones, M.K. A cytochrome b561 with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum. PLoS Negl. Trop. Dis. 4 (2010) e884. [PMID: 21103361]
Accepted name: tetrahydromethanopterin S-methyltransferase
Reaction: 5-methyl-5,6,7,8-tetrahydromethanopterin + CoM + 2 Na+[side 1] = 5,6,7,8-tetrahydromethanopterin + 2-(methylsulfanyl)ethane-1-sulfonate + 2 Na+[side 2]
For diagram of reaction click here
Glossary: CoM = coenzyme M = 2-sulfanylethane-1-sulfonate
tetrahydromethanopterin = 1-(4-{(1R)-1-[(6S,7S)-2-amino-7-methyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]ethylamino}phenyl)-1-deoxy-5-O-{5-O-[(1S)-1,3-dicarboxypropylphosphonato]-α-D-ribofuranosyl}-D-ribitol
Other name(s): tetrahydromethanopterin methyltransferase; mtrA-H (gene names); cmtA (gene name); N5-methyltetrahydromethanopterin—coenzyme M methyltransferase; 5-methyl-5,6,7,8-tetrahydromethanopterin:2-mercaptoethanesulfonate 2-methyltransferase
Systematic name: 5-methyl-5,6,7,8-tetrahydromethanopterin:CoM 2-methyltransferase (Na+-transporting)
Comments: Involved in the formation of methane from CO2 in methanogenic archaea. The reaction involves the export of one or two sodium ions. The enzyme from the archaeon Methanobacterium thermoautotrophicum is a membrane-associated multienzyme complex composed of eight different subunits, and contains a 5'-hydroxybenzimidazolyl-cobamide cofactor, to which the methyl group is attached during the transfer. A soluble enzyme that is induced by the presence of CO has been reported as well [6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sauer, F.D. Tetrahydromethanopterin methyltransferase, a component of the methane synthesizing complex of Methanobacterium thermoautotrophicum. Biochem. Biophys. Res. Commun. 136 (1986) 542-547. [PMID: 3085670]
2. Gartner, P., Ecker, A., Fischer, R., Linder, D., Fuchs, G. and Thauer, R.K. Purification and properties of N5-methyltetrahydromethanopterin:coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Eur. J. Biochem. 213 (1993) 537-545. [PMID: 8477726]
3. Weiss, D.S., Gartner, P. and Thauer, R.K. The energetics and sodium-ion dependence of N5-methyltetrahydromethanopterin:coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor. Eur. J. Biochem. 226 (1994) 799-809. [PMID: 7813469]
4. Harms, U., Weiss, D.S., Gartner, P., Linder, D. and Thauer, R.K. The energy conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits. Eur. J. Biochem. 228 (1995) 640-648. [PMID: 7737157]
5. Gottschalk, G. and Thauer, R.K. The Na+-translocating methyltransferase complex from methanogenic archaea. Biochim. Biophys. Acta 1505 (2001) 28-36. [PMID: 11248186]
6. Vepachedu, V.R. and Ferry, J.G. Role of the fused corrinoid/methyl transfer protein CmtA during CO-dependent growth of Methanosarcina acetivorans. J. Bacteriol. 194 (2012) 4161-4168. [PMID: 22636775]
EC 7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.2.2.1 Na+-transporting two-sector ATPase
Accepted name: Na+-transporting two-sector ATPase
Reaction: ATP + H2O + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
Other name(s): sodium-transporting two-sector ATPase; Na+-translocating ATPase; Na+-translocating FoF1-ATPase; sodium ion specific ATP synthase
Systematic name: ATP phosphohydrolase (two-sector, Na+-transporting)
Comments: A multisubunit ATPase transporter found in some halophilic or alkalophilic bacteria that functions in maintaining sodium homeostasis. The enzyme is similar to EC 7.1.2.2 (H+-transporting two-sector ATPase) but pumps Na+ rather than H+. By analogy to EC 7.1.2.2, it is likely that the enzyme pumps 4 sodium ions for every ATP molecule that is hydrolysed. cf. EC 7.2.2.3, P-type Na+ transporter and EC 7.2.2.4, ABC-type Na+ transporter.
Links to other databases:
BRENDA,
EXPASY,
IUBMB,
KEGG,
MetaCyc,
PDB,
CAS Registry Number:
References:
1. Solioz, M. and Davies, K. Operon of vacuolar-type Na+-ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 9453-9459. [PMID: 8144530]
2. Takase, K., Kakinuma, S., Yamato, I., Konishi, K., Igarashi, K. and Kanikuma, Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 11037-11044. [PMID: 8157629]
3. Rahlfs, S. and Müller, V. Sequence of subunit c of the Na+-translocating F1Fo-ATPase of Acetobacterium woodii: proposal for determinants of Na+ specificity as revealed by sequence comparisons. FEBS Lett. 404 (1997) 269-271. [PMID: 9119076]
Accepted name: ABC-type Cd2+ transporter
Reaction: ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2]
Other name(s): cadmium-transporting ATPase (ambiguous); ABC-type cadmium-transporter
Systematic name: ATP phosphohydrolase (ABC-type, heavy-metal-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509-6517. [PMID: 8626454]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: P-type Na+ transporter
Reaction: ATP + H2O + Na+[side 1] = ADP + phosphate + Na+[side 2]
Other name(s): Na+-exporting ATPase (ambiguous); ENA1 (gene name); ENA2 (gene name); ENA5 (gene name)
Systematic name: ATP phosphohydrolase (P-type, Na+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed. Some forms can also export Li+ ions. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.4, ABC-type Na+ transporter.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Wieland, J., Nitsche, A.M., Strayle, J., Steiner, H. and Rudolph, H.K. The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane. EMBO J. 14 (1995) 3870-3882. [PMID: 7664728]
2. Catty, P., de Kerchove d'Exaerde, A. and Goffeau, A. The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett. 409 (1997) 325-332. [PMID: 9224683]
3. Benito, B., Quintero, F.J. and Rodriguez-Navarro, A. Overexpression of the sodium ATPase of Saccharomyces cerevisiae: conditions for phosphorylation from ATP and Pi. Biochim. Biophys. Acta 1328 (1997) 214-226. [PMID: 9315618]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type Na+ transporter
Reaction: ATP + H2O + Na+[side 1] = ADP + phosphate + Na+[side 2]
Other name(s): natAB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, Na+-exporting)
Comments: ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This bacterial enzyme, characterized from Bacillus subtilis, exports Na+ ions out of the cell. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.3, P-type Na+ transporter.
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BRENDA,
EXPASY,
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Metacyc,
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References:
1. Cheng, J., Guffanti, A.A. and Krulwich, T.A. A two-gene ABC-type transport system that extrudes Na+ in Bacillus subtilis is induced by ethanol or protonophore. Mol. Microbiol. 23 (1997) 1107-1120. [PMID: 9106203]
2. Ogura, M., Tsukahara, K., Hayashi, K. and Tanaka, T. The Bacillus subtilis NatK-NatR two-component system regulates expression of the natAB operon encoding an ABC transporter for sodium ion extrusion. Microbiology 153 (2007) 667-675. [PMID: 17322186]
Accepted name: ABC-type Mn2+ transporter
Reaction: ATP + H2O + Mn2+-[manganese-binding protein][side 1] = ADP + phosphate + Mn2+[side 2] + [manganese-binding protein][side 1]
Other name(s): ABC-type manganese permease complex; manganese-transporting ATPase (ambiguous); ABC-type manganese transporter
Systematic name: ATP phosphohydrolase (ABC-type, Mn2+-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of Mn2+, Zn2+ and iron chelates.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Novak, R., Braun, J.S., Charpentier, E. and Tuomanen, E. Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa. Mol. Microbiol. 29 (1998) 1285-1296. [PMID: 9767595]
4. Kolenbrander, P.E., Andersen, R.N., Baker, R.A. and Jenkinson, H.F. The adhesion-assoiated aca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn2+ uptake. J. Bacteriol. 180 (1998) 290-295. [PMID: 9440518]
Accepted name: P-type K+ transporter
Reaction: ATP + H2O + K+[side 1] = ADP + phosphate + K+[side 2]
Other name(s): K+-translocating Kdp-ATPase; multi-subunit K+-transport ATPase; K+-transporting ATPase; potassium-importing ATPase; K+-importing ATPase
Systematic name: ATP phosphohydrolase (P-type, K+-importing)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that is involved in K+ import. The probable stoichiometry is one ion per ATP hydrolysed.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
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References:
1. Siebers, A. and Altendorf, K. Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli. J. Biol. Chem. 264 (1989) 5831-5838. [PMID: 2522440]
2. Gassel, M., Siebers, A., Epstein, W. and Altendorf, K. Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of Escherichia coli. Biochim. Biophys. Acta 1415 (1998) 77-84. [PMID: 9858692]
3. Huang, C.S., Pedersen, B.P. and Stokes, D.L. Crystal structure of the potassium-importing KdpFABC membrane complex. Nature 546 (2017) 681-685. [PMID: 28636601]
Accepted name: ABC-type Fe3+ transporter
Reaction: ATP + H2O + Fe3+-[iron-binding protein][side 1] = ADP + phosphate + Fe3+[side 2] + [iron-binding protein][side 1]
Other name(s): Fe3+-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, Fe3+-transporting)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. A bacterial enzyme that interacts with a periplasmic iron-binding protein to imports Fe3+ ions into the cytoplasm.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Angerer, A., Klupp, B. and Braun, V. Iron transport systems of Serratia marcescens. J. Bacteriol. 174 (1992) 1378-1387. [PMID: 1531225]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Khun, H.H., Kirby, S.D. and Lee, B.C. A Neisseria meningitidis fbp ABC mutant is incapable of using nonheme iron for growth. Infect. Immun. 66 (1998) 2330-2336. [PMID: 9573125]
Accepted name: P-type Cu+ transporter
Reaction: ATP + H2O + Cu+[side 1] = ADP + phosphate + Cu+[side 2]
Other name(s): Cu+-exporting ATPase (ambiguous); copA (gene name); ATP7A (gene name); ATP7B (gene name)
Systematic name: ATP phosphohydrolase (P-type, Cu+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme transports Cu+ or Ag+, and cannot transport the divalent ions, contrary to EC 7.2.2.9, P-type Cu2+ transporter, which mainly transports the divalent copper ion.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Fan, B. and Rosen, B.P. Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase. J. Biol. Chem. 277 (2002) 46987-46992. [PMID: 12351646]
2. Banci, L., Bertini, I., Ciofi-Baffoni, S., D'Onofrio, M., Gonnelli, L., Marhuenda-Egea, F.C. and Ruiz-Duenas, F.J. Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states. J. Mol. Biol. 317 (2002) 415-429. [PMID: 11922674]
3. Mandal, A.K. and Arguello, J.M. Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu+-ATPase CopA. Biochemistry 42 (2003) 11040-11047. [PMID: 12974640]
4. Gonzalez-Guerrero, M. and Arguello, J.M. Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites. Proc. Natl. Acad. Sci. USA 105 (2008) 5992-5997. [PMID: 18417453]
5. Lewis, D., Pilankatta, R., Inesi, G., Bartolommei, G., Moncelli, M.R. and Tadini-Buoninsegni, F. Distinctive features of catalytic and transport mechanisms in mammalian sarco-endoplasmic reticulum Ca2+ ATPase (SERCA) and Cu+ (ATP7A/B) ATPases. J. Biol. Chem. 287 (2012) 32717-32727. [PMID: 22854969]
6. Tadini-Buoninsegni, F., Bartolommei, G., Moncelli, M.R., Pilankatta, R., Lewis, D. and Inesi, G. ATP dependent charge movement in ATP7B Cu+-ATPase is demonstrated by pre-steady state electrical measurements. FEBS Lett. 584 (2010) 4619-4622. [PMID: 20965182]
7. Mattle, D., Sitsel, O., Autzen, H.E., Meloni, G., Gourdon, P. and Nissen, P. On allosteric modulation of P-type Cu+-ATPases. J. Mol. Biol. 425 (2013) 2299-2308. [PMID: 23500486]
Accepted name: P-type Cu2+ transporter
Reaction: ATP + H2O + Cu2+[side 1] = ADP + phosphate + Cu2+[side 2]
Other name(s): Cu2+-exporting ATPase; copB (gene name)
Systematic name: ATP phosphohydrolase (P-type, Cu2+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].
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BRENDA,
EXPASY,
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Metacyc,
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References:
1. Mana-Capelli, S., Mandal, A.K. and Arguello, J.M. Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain. J. Biol. Chem. 278 (2003) 40534-40541. [PMID: 12876283]
2. Jayakanthan, S., Roberts, S.A., Weichsel, A., Arguello, J.M. and McEvoy, M.M. Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle. Biosci Rep 32 (2012) 443-453. [PMID: 22663904]
Accepted name: P-type Ca2+ transporter
Reaction: ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2]
Other name(s): sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca2+-ATPase; calcium pump; Ca2+-pumping ATPase; plasma membrane Ca-ATPase; Ca2+-transporting ATPaseP-
Systematic name: ATP phosphohydrolase (P-type, Ca2+-transporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca2+ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).
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EXPASY,
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Metacyc,
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References:
1. Schatzmann, H.J. and Vicenzi, F.F. Calcium movements across the membrane of human red cells. J. Physiol. 201 (1969) 369-395. [PMID: 4238381]
2. Inesi, G., Watanabe, T., Coan, C. and Murphy, A. The mechanism of sarcoplasmic reticulum ATPase. Ann. N.Y. Acad. Sci. 402 (1982) 515-532. [PMID: 6301340]
3. Carafoli, E. The Ca2+ pump of the plasma membrane. J. Biol. Chem. 267 (1992) 2115-2118. [PMID: 1310307]
4. MacLennan, D.H., Rice, W.J. and Green, N.M. The mechanism of Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases. J. Biol. Chem. 272 (1997) 28815-28818. [PMID: 9360942]
5. Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647-655. [PMID: 10864315]
6. Andersen, J.L., Gourdon, P., Moller, J.V., Morth, J.P. and Nissen, P. Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 718-722. [PMID: 21636921]
Accepted name: ABC-type Ni2+ transporter
Reaction: ATP + H2O + Ni2+-[nickel-binding protein][side 1] = ADP + phosphate + Ni2+[side 2] + [nickel-binding protein][side 1]
Other name(s): nickel ABC transporter; nickel-transporting ATPase; ABC-type nickel-transporter
Systematic name: ATP phosphohydrolase (ABC-type, Ni2+-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of Ni2+; the identity of the nickel species transported has not been conclusively established. Does not undergo phosphorylation during the transport process.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Hendricks, J.K. and Mobley, H.L. Helicobacter pylori ABC transporter: effect of allelic exchange mutagenesis on urease activity. J. Bacteriol. 179 (1997) 5892-5902. [PMID: 9294450]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: P-type Zn2+ transporter
Reaction: ATP + H2O + Zn2+[side 1] = ADP + phosphate + Zn2+[side 2]
Other name(s): Zn(II)-translocating P-type ATPase; Zn2+-exporting ATPase; P1B-type ATPase; HMA4 (gene name); zntA (gene name)
Systematic name: ATP phosphohydrolase (P-type, Zn2+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme, present in prokaryotes and photosynthetic eukaryotes, exports Zn2+ and the related cations Cd2+ and Pb2+.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Beard, S.J., Hashim, R., Membrillo-Hernández, J., Hughes, M.N. and Poole, R.K. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase. Mol. Microbiol. 25 (1997) 883-891. [PMID: 9364914]
2. Rensing, C., Mitra, B. and Rosen, B.P. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc. Natl. Acad. Sci. USA 94 (1997) 14326-14331. [PMID: 9405611]
3. Rensing, C., Sun, Y., Mitra, B. and Rosen, B.P. Pb(II)-translocating P-type ATPases. J. Biol. Chem. 273 (1998) 32614-32617. [PMID: 9830000]
4. Mills, R.F., Francini, A., Ferreira da Rocha, P.S., Baccarini, P.J., Aylett, M., Krijger, G.C. and Williams, L.E. The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in
detoxification of transition metals supplied at elevated levels. FEBS Lett. 579 (2005) 783-791. [PMID: 15670847]
5. Eren, E. and Argüello, J.M. Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasis. Plant Physiol. 136 (2004) 3712-3723. [PMID: 15475410]
Accepted name: Na+/K+-exchanging ATPase
Reaction: ATP + H2O + Na+[side 1] + K+[side 2] = ADP + phosphate + Na+[side 2] + K+[side 1]
Other name(s): (Na+ + K+)-activated ATPase; Na,K-activated ATPase; Na,K-pump; Na+,K+-ATPase; sodium/potassium-transporting ATPase; Na+/K+-exchanging ATPase
Systematic name: ATP phosphohydrolase (P-type, Na+/K+-exchanging)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na+ and influx of two K+ per ATP hydrolysed. It is involved in generating the plasma membrane electrical potential.
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Metacyc,
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References:
1. Skou, J.C. The influence of some cations on an adenosinetriphosphatase from peripheral nerve. Biochim. Biophys. Acta 23 (1957) 394-401. [PMID: 13412736]
2. Post, R.L., Sen, A.K. and Rosenthal, A.S. A phosphorylated intermediate in adenosine triphosphate-dependent sodium and potassium transport across kidney membrane. J. Biol. Chem. 240 (1965) 1437-1445. [PMID: 14284759]
3. Skou, J.C. The energy-coupled exchange of Na+ for K+ across the cell membrane. The Na+,K+ pump. FEBS Lett. 268 (1990) 314-324. [PMID: 2166689]
4. Castillo, J.P., Rui, H., Basilio, D., Das, A., Roux, B., Latorre, R., Bezanilla, F. and Holmgren, M. Mechanism of potassium ion uptake by the Na(+)/K(+)-ATPase. Nat Commun 6 (2015) 7622. [PMID: 26205423]
Accepted name: P-type Mg2+ transporter
Reaction: ATP + H2O + Mg2+[side 1] = ADP + phosphate + Mg2+[side 2]
Other name(s): Mg2+-transporting P-type ATPase; Mg2+-transporting ATPase; Mg2+-importing ATPase; magnesium-translocating P-type ATPase; mgtA (gene name); mgtB (gene name)
Systematic name: ATP phosphohydrolase (P-type, Mg2+-importing)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that imports Mg2+ with, rather than against, the Mg2+ electrochemical gradient. The enzyme is also involved in Ni2+ import.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Snavely, M.D., Miller, C.G. and Maguire, M.E. The mgtB Mg2+ transport locus of Salmonella typhimurium encodes a P-type ATPase. J. Biol. Chem 266 (1991) 815-823. [PMID: 1824701]
2. Maguire, M.E. MgtA and MgtB: prokaryotic P-type ATPases that mediate Mg2+ influx. J. Bioenerg. Biomembr. 24 (1992) 319-328. [PMID: 1328179]
3. Tao, T., Snavely, M.D., Farr, S.G. and Maguire, M.E. Magnesium transport in Salmonella typhimurium: mtgA encodes a P-type ATPase and is regulated by Mg2+ in a manner similar to that of the mgtB P-type ATPase. J. Bacteriol. 177 (1995) 2654-2662. [PMID: 7751273]
Accepted name: P-type Ag+ transporter
Reaction: ATP + H2O + Ag+[side 1] = ADP + phosphate + Ag+[side 2]
Other name(s): Ag+-exporting ATPase
Systematic name: ATP phosphohydrolase (P-type, Ag+-exporting)
Comments: A P-type ATPase that exports Ag+ ions from some bacteria, archaea as well as from some animal tissues. The proteins also transport Cu+ ions (cf. , P-type Cu+ transporter).
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BRENDA,
EXPASY,
KEGG,
Metacyc,
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References:
1. Gupta, A., Matsui, K., Lo, J.F. and Silver, S. Molecular basis for resistance to silver cations in Salmonella. Nature Med. 5 (1999) 183-188. [PMID: 9930866]
2. Bury, N.R., Grosell, M., Grover, A.K. and Wood, C.M. ATP-dependent silver transport across the basolateral membrane of rainbow trout gills. Toxicol. Appl. Pharmacol. 159 (1999) 1-8. [PMID: 10448119]
Accepted name: ABC-type ferric hydroxamate transporter
Reaction: ATP + H2O + Fe3+-hydroxamate complex-[hydroxamate-binding protein][side 1] = ADP + phosphate + Fe3+-hydroxamate complex[side 2] + [hydroxamate-binding protein][side 1]
Other name(s): iron(III) hydroxamate transporting ATPase; iron(III) hydroxamate ABC transporter; fhuCDB (gene names)
Systematic name: ATP phosphohydrolase [ABC-type, iron(III) hydroxamate-importing]
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of Fe3+-complexed hydroxamate siderophores such as coprogen, ferrichrome and the ferric hydroxamate antibiotic, albomycin.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Koster, W. Iron(III) hydroxamate transport across the cytoplasmic membrane of Escherichia coli. Biol. Met. 4 (1991) 23-32. [PMID: 1830209]
2. Speziali, C.D., Dale, S.E., Henderson, J.A., Vines, E.D. and Heinrichs, D.E. Requirement of Staphylococcus aureus ATP-binding cassette-ATPase FhuC for iron-restricted growth and evidence that it functions with more than one iron transporter. J. Bacteriol. 188 (2006) 2048-2055. [PMID: 16513734]
Accepted name: ABC-type ferric enterobactin transporter
Reaction: ATP + H2O + Fe3+-enterobactin complex-[enterobactin-binding protein][side 1] = ADP + phosphate + Fe3+-enterobactin complex[side 2] + [enterobactin-binding protein][side 1]
Other name(s): ferric enterobactin transporting ATPase; ferric enterobactin ABC transporter; fepBCDG (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, iron(III) enterobactin-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of Fe3+-enterobactin complexes.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Chenault, S.S. and Earhart, C.F. Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease. Mol. Microbiol. 5 (1991) 1405-1413. [PMID: 1787794]
2. Shea, C.M. and McIntosh, M.A. Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding-protein-dependent systems in Escherichia coli. Mol. Microbiol. 5 (1991) 1415-1428. [PMID: 1838574]
Accepted name: ABC-type ferric citrate transporter
Reaction: ATP + H2O + Fe3+-dicitrate-[dicitrate-binding protein][side 1] = ADP + phosphate + Fe3+-dicitrate[side 2] + [dicitrate-binding protein][side 1]
Other name(s): ferric citrate transporting ATPase; ferric citrate ABC transporter; fecBCDE (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, iron(III) dicitrate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichia coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of Fe3+-citrate in the form of a mononuclear (containing one iron(III) ion and two citrate molecules) or dinuclear (containing 2 iron(III) ions) complexes.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Staudenmaier, H., Van Hove, B., Yaraghi, Z. and Braun, V. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. J. Bacteriol. 171 (1989) 2626-2633. [PMID: 2651410]
2. Banerjee, S., Paul, S., Nguyen, L.T., Chu, B.C. and Vogel, H.J. FecB, a periplasmic ferric-citrate transporter from E. coli, can bind different forms of ferric-citrate as well as a wide variety of metal-free and metal-loaded tricarboxylic acids. Metallomics 8 (2016) 125-133. [PMID: 26600288]
Accepted name: H+/K+-exchanging ATPase
Reaction: ATP + H2O + H+[side 1] + K+[side 2] = ADP + phosphate + H+[side 2] + K+[side 1]
Other name(s): H+-K+-ATPase; H,K-ATPase; (K+ + H+)-ATPase
Systematic name: ATP phosphohydrolase (P-type,H+/K+-exchanging)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A gastric mucosal enzyme that catalyses the efflux of one H+ and the influx of one K+ per ATP hydrolysed.
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EXPASY,
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MetaCyc,
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References:
1. Sachs, G., Collier, R.H., Shoemaker, R.L. and Hirschowitz, B.I. The energy source for gastric H+ secretion. Biochim. Biophys. Acta 162 (1968) 210-219. [PMID: 5682852]
2. Hersey, S.J., Perez, A. Matheravidathu, S. and Sachs, G. Gastric H+-K+-ATPase in situ: evidence for compartmentalization. Am. J. Physiol. 257 (1989) G539-G547. [PMID: 2552824]
3. Rabon, E.C. and Reuben, M.A. The mechanism and structure of the gastric H,K-ATPase. Annu. Rev. Physiol. 52 (1990) 321-344. [PMID: 2158765]
Accepted name: ABC-type Zn2+ transporter
Reaction: ATP + H2O + Zn2+-[zinc-binding protein][side 1] = ADP + phosphate + Zn2+[side 2] + [zinc-binding protein][side 1]
Other name(s): Zn2+-transporting ATPase; Zn2+ ABC transporter; znuABC (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, Zn2+-importing)
Comments: ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of Zn2+.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Patzer, S.I. and Hantke, K. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28 (1998) 1199-1210. [PMID: 9680209]
2. Hantke, K. Bacterial zinc uptake and regulators. Curr Opin Microbiol 8 (2005) 196-202. [PMID: 15802252]
Accepted name: Cd2+-exporting ATPase
Reaction: ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2]
Other name(s): cadmium-translocating P-type ATPase; cadmium-exporting ATPase
Systematic name: ATP phosphohydrolase (Cd2+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants.
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References:
1. Silver, S. and Ji, G. Newer systems for bacterial resistance to toxic heavy metals. Environ. Health Perspect. 102, Suppl. 3 (1994) 107-113. [PMID: 7843081]
2. Tsai, K.J. and Linet, A.L. Formation of a phosphorylated enzyme intermediate by the cadA Cd2+-ATPase. Arch. Biochem. Biophys. 305 (1993) 267-270. [PMID: 8373163]
Accepted name: P-type Mn2+ transporter
Reaction: ATP + H2O + Mn2+[side 1] = ADP + phosphate + Mn2+[side 2]
Other name(s): Mn(II)-translocating P-type ATPase; Mn2+-exporting ATPase; P1B-type ATPase (ambiguous); ctpC (gene name)
Systematic name: ATP phosphohydrolase (P-type, Mn2+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme, detected in mycobacteria, is a high affinity slow turnover ATPase exporting Mn2+.
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References:
1. Padilla-Benavides, T., Long, J.E., Raimunda, D., Sassetti, C.M. and Arguello, J.M. A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria. J. Biol. Chem. 288 (2013) 11334-11347. [PMID: 23482562]
Accepted name: Na+-exporting diphosphatase
Reaction: diphosphate + H2O + Na+[side 1] = 2 phosphate + Na+[side 2]
Other name(s): Na+-translocating membrane pyrophosphatase; sodium-translocating pyrophosphatase
Systematic name: diphosphate phosphohydrolase (Na+-transporting)
Comments: Requires Na+ and K+. This enzyme, found in some bacteria and archaea, couples the energy from diphosphate hydrolysis to active sodium translocation across the membrane. The enzyme is electrogenic, as the Na+ transport results in generation of a positive potential in the inner side of the membrane.
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References:
1. Belogurov, G.A., Malinen, A.M., Turkina, M.V., Jalonen, U., Rytkonen, K., Baykov, A.A. and Lahti, R. Membrane-bound pyrophosphatase of Thermotoga maritima requires sodium for activity. Biochemistry 44 (2005) 2088-2096. [PMID: 15697234]
2. Malinen, A.M., Belogurov, G.A., Baykov, A.A. and Lahti, R. Na+-pyrophosphatase: a novel primary sodium pump. Biochemistry 46 (2007) 8872-8878. [PMID: 17605473]
3. Luoto, H.H., Belogurov, G.A., Baykov, A.A., Lahti, R. and Malinen, A.M. Na+-translocating membrane pyrophosphatases are widespread in the microbial world and evolutionarily precede H+-translocating pyrophosphatases. J. Biol. Chem. 286 (2011) 21633-21642. [PMID: 21527638]
Contents
EC 7.2.4 Linked to decarboxylation
EC 7.2.4.1 carboxybiotin decarboxylase
Accepted name: carboxybiotin decarboxylase
Reaction: a carboxybiotinyl-[protein] + n Na+[side 1] + H+[side 2] = CO2 + a biotinyl-[protein] + n Na+[side 2] (n = 1-2)
For diagram of the reaction click here
Other name(s): MadB; carboxybiotin protein decarboxylase
Systematic name: carboxybiotinyl-[protein] carboxy-lyase
Comments: The integral membrane protein MadB from the anaerobic bacterium Malonomonas rubra is a component of the multienzyme complex EC 4.1.1.89, biotin-dependent malonate decarboxylase. The free energy of the decarboxylation reaction is used to pump Na+ out of the cell. The enzyme is a member of the Na+-translocating decarboxylase family, other members of which include EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)] and EC 7.2.4.3 [(S)-methylmalonyl-CoA decarboxylase (sodium-transporting)] [2].
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References:
1. Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103-115. [PMID: 9128730]
2. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]
Accepted name: oxaloacetate decarboxylase (Na+ extruding)
Reaction: oxaloacetate + 2 Na+[side 1] = pyruvate + CO2 + 2 Na+[side 2]
Other name(s): oxaloacetate β-decarboxylase (ambiguous); oxalacetic acid decarboxylase (ambiguous); oxalate β-decarboxylase (ambiguous); oxaloacetate carboxy-lyase (ambiguous)
Systematic name: oxaloacetate carboxy-lyase (pyruvate-forming; Na+-extruding)
Comments: The enzyme from the bacterium Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+. Differs from EC 4.1.1.112 (oxaloacetate decarboxylase) for which there is no evidence for involvement in Na+ transport.
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References:
1. Dimroth, P. Characterization of a membrane-bound biotin-containing enzyme: oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 115 (1981) 353-358. [PMID: 7016536]
2. Dimroth, P. The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 121 (1982) 435-441. [PMID: 7037395]
Accepted name: (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)
Reaction: (S)-methylmalonyl-CoA + Na+[side 1] + H=[side 2] = propanoyl-CoA + CO2 + Na+[side 2]
Other name(s): methylmalonyl-coenzyme A decarboxylase (ambiguous); (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase (ambiguous)
Systematic name: (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming, sodium-transporting)
Comments: This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.
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References:
1. Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253-1261. [PMID: 5646172]
2. Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient. Nature 296 (1982) 584-585. [PMID: 7070502]
3. Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645-650. [PMID: 2920730]
4. Huder, J.B. and Dimroth, P. Expression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase from Veillonella parvula and of mutated enzyme specimens in Escherichia coli. J. Bacteriol. 177 (1995) 3623-3630. [PMID: 7601825]
5. Bott, M., Pfister, K., Burda, P., Kalbermatter, O., Woehlke, G. and Dimroth, P. Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and sequencing of the structural genes and purification of the enzyme complex. Eur. J. Biochem. 250 (1997) 590-599. [PMID: 9428714]
Accepted name: biotin-dependent malonate decarboxylase
Reaction: malonate + H+ + Na+ [side 1] = acetate + CO2 + Na+ [side 2]
For diagram of the reaction click here
Other name(s): malonate decarboxylase (with biotin); malonate decarboxylase (ambiguous)
Systematic name: malonate carboxy-lyase (biotin-dependent)
Comments: Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes. The enzyme described here is a membrane-bound biotin-dependent, Na+-translocating enzyme [6]. The other type is a biotin-independent cytosolic protein (cf. EC 4.1.1.88, biotin-independent malonate decarboxylase). As free malonate is chemically rather inert, it has to be activated prior to decarboxylation. Both enzymes achieve this by exchanging malonate with an acetyl group bound to an acyl-carrier protiein (ACP), to form malonyl-ACP and acetate, with subsequent decarboxylation regenerating the acetyl-bound form of the enzyme. The ACP subunit of both enzymes differs from that found in fatty-acid biosynthesis by having phosphopantethine attached to a serine side-chain as 2-(5-triphosphoribosyl)-3-dephospho-CoA rather than as phosphopantetheine 4'-phosphate. In the anaerobic bacterium Malonomonas rubra, the components of the multienzyme complex/enzymes involved in carrying out the reactions of this enzyme are as follows: MadA (EC 2.3.1.187, acetyl-S-ACP:malonate ACP transferase), MadB (EC 7.2.4.1, carboxybiotin decarboxylase), MadC/MadD (EC 2.1.3.10, malonyl-S-ACP:biotin-protein carboxyltransferase) and MadH (EC 6.2.1.35, acetate--[acyl-carrier protein] ligase). Two other components that are involved are MadE, the acyl-carrier protein and MadF, the biotin protein. The carboxy group is lost with retention of configuration [5].
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References:
1. Hilbi, H., Dehning, I., Schink, B. and Dimroth, P. Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur. J. Biochem. 207 (1992) 117-123. [PMID: 1628643]
2. Hilbi, H. and Dimroth, P. Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase. Arch. Microbiol. 162 (1994) 48-56. [PMID: 18251085]
3. Berg, M., Hilbi, H. and Dimroth, P. The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2'-(5"-phosphoribosyl)-3'-dephosphocoenzyme A as a prosthetic group. Biochemistry 35 (1996) 4689-4696. [PMID: 8664258]
4. Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103-115. [PMID: 9128730]
5. Micklefield, J., Harris, K.J., Gröger, S., Mocek, U., Hilbi, H., Dimroth, P. and Floss, H.G. Stereochemical course of malonate decarboxylase in Malonomonas rubra has biotin decarboxylation with retention. J. Am. Chem. Soc. 117 (1995) 1153-1154.
6. Kim, Y.S. Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application. J. Biochem. Mol. Biol. 35 (2002) 443-451. [PMID: 12359084]
7. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]
Accepted name: glutaconyl-CoA decarboxylase
Reaction: (2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
Glossary: (E)-glutaconyl-CoA = (2E)-4-carboxybut-2-enoyl-CoA
Other name(s): glutaconyl coenzyme A decarboxylase; pent-2-enoyl-CoA carboxy-lyase; 4-carboxybut-2-enoyl-CoA carboxy-lyase
Systematic name: (2E)-4-carboxybut-2-enoyl-CoA carboxy-lyase [(2E)-but-2-enoyl-CoA-forming]
Comments: The enzyme from the bacterium Acidaminococcus fermentans is a biotinyl-protein, requires Na+, and acts as a sodium pump. Prior to the Na+-dependent decarboxylation, the carboxylate is transferred to biotin in a Na+-independent manner. The conserved lysine, to which biotin forms an amide bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme.
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References:
1. Buckel, W.S. and Semmler, R. Purification, characterisation and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria. Eur. J. Biochem. 136 (1983) 427-434. [PMID: 6628393]
2. Buckel, W. Sodium ion-translocating decarboxylases. Biochim. Biophys. Acta 1505 (2001) 15-27. [PMID: 11248185]
EC 7.3.2 Linked to the hydrolysis of a nucleoside triphosphate
Contents
EC 7.3.2.1 ABC-type phosphate transporter
Accepted name: ABC-type phosphate transporter
Reaction: ATP + H2O + phosphate-[phosphate-binding protein][side 1] = ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
Other name(s): phosphate ABC transporter; phosphate-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, phosphate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of phosphate anions. Unlike P-type ATPases, it does not undergo phosphorylation during the transport process.
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References:
1. Webb, D.C., Rosenberg, H. and Cox, G.B. Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. A role for proline residues in transmembrane helices. J. Biol. Chem. 267 (1992) 24661-24668. [PMID: 1447208]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Braibant, M., LeFevre, P., de Wit, L., Ooms, J., Peirs, P., Huygen, K., Wattiez, R. and Content, J. Identification of a second Mycobacterium tuberculosis gene cluster encoding proteins of an ABC phosphate transporter. FEBS Lett. 394 (1996) 206-212. [PMID: 8843165]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type phosphonate transporter
Reaction: ATP + H2O + phosphonate-[phosphonate-binding protein][side 1] = ADP + phosphate + phosphonate[side 2] + [phosphonate-binding protein][side 1]
Other name(s): phosphonate-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, phosphonate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of phosphonate and organophosphate anions.
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References:
1. Wanner, B.L. and Metcalf, W.W. Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation. FEMS Microbiol. Lett. 79 (1992) 133-139. [PMID: 1335942]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type sulfate transporter
Reaction: ATP + H2O + sulfate-[sulfate-binding protein][side 1] = ADP + phosphate + sulfate[side 2] + [sulfate-binding protein][side 1]
Other name(s): sulfate ABC transporter; sulfate-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, sulfate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichia coli can interact with either of two periplasmic binding proteins and mediates the high affinity uptake of sulfate and thiosulfate. May also be involved in the uptake of selenite, selenate and possibly molybdate. Does not undergo phosphorylation during the transport.
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References:
1. Sirko, A., Zatyka, M., Sadowy, E. and Hulanicka, D. Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins. J. Bacteriol. 177 (1995) 4134-4136. [PMID: 7608089]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type nitrate transporter
Reaction: ATP + H2O + nitrate-[nitrate-binding protein][side 1] = ADP + phosphate + nitrate[side 2] + [nitrate-binding protein][side 1]
Other name(s): nitrate-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, nitrate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins.The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of nitrate, nitrite, and cyanate.
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References:
1. Omata, T. Structure, function and regulation of the nitrate transport system of the cyanobacterium Synechococcus sp. PCC7942. Plant Cell Physiol. 36 (1995) 207-213. [PMID: 7767600]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type molybdate transporter
Reaction: ATP + H2O + molybdate-[molybdate-binding protein][side 1] = ADP + phosphate + molybdate[side 2] + [molybdate-binding protein][side 1]
Glossary: molybdate = tetraoxidomolybdate(2-) = MoO42-
Other name(s): molybdate ABC transporter; molybdate-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, molybdate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of molybdate and tungstate. Does not undergo phosphorylation during the transport process.
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References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Grunden, A.M. and Shanmugam, K.T. Molybdate transport and regulation in bacteria. Arch. Mikrobiol. 168 (1997) 345-354. [PMID: 9325422]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type tungstate transporter
Reaction: ATP + H2O + tungstate-[tungstate-binding protein][side 1] = ADP + phosphate + tungstate[side 2] + [tungstate-binding protein][side 1]
Other name(s): tungstate transporter; tungstate-importing ATPase; tungstate-specific ABC transporter; WtpABC; TupABC
Systematic name: ATP phosphohydrolase (ABC-type, tungstate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, characterized from the archaeon Pyrococcus furiosus, the Gram-positive bacterium Eubacterium acidaminophilum and the Gram-negative bacterium Campylobacter jejuni, interacts with an extracytoplasmic substrate binding protein and mediates the import of tungstate into the cell for incorporation into tungsten-dependent enzymes.
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References:
1. Makdessi, K., Andreesen, J.R. and Pich, A. Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. J. Biol. Chem. 276 (2001) 24557-24564. [PMID: 11292832]
2. Bevers, L.E., Hagedoorn, P.L., Krijger, G.C. and Hagen, W.R. Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. J. Bacteriol. 188 (2006) 6498-6505. [PMID: 16952940]
3. Smart, J.P., Cliff, M.J. and Kelly, D.J. A role for tungsten in the biology of Campylobacter jejuni: tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter. Mol. Microbiol. 74 (2009) 742-757. [PMID: 19818021]
Accepted name: arsenite-transporting ATPase
Reaction: ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]
Other name(s): arsAB (gene names)
Systematic name: ATP phosphohydrolase (arsenite-exporting)
Comments: This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family. The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions.
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References:
1. Silver, S., Misra, T.K. and Laddaga, R.A. DNA sequence analysis of bacterial toxic heavy metal resistance. Biol. Trace Elem. Res. 21 (1989) 145-163. [PMID: 2484581]
2. Rosen, B.P., Weigel, U., Monticello, R.A. and Edwards, B.P. Molecular analysis of an anion pump: purification of the ArsC protein. Arch. Biochem. Biophys. 284 (1991) 381-385. [PMID: 1703401]
3. Bruhn, D.F., Li, J., Silver, S., Roberto, F. and Rosen, B.P. The arsenical resistance operon of IncN plasmid R46. FEMS Microbiol. Lett. 139 (1996) 149-153. [PMID: 8674982]
4. Zhou, T., Rosen, B.P. and Gatti, D.L. Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 921-924. [PMID: 10089335]
EC 7.4.2 Linked to the hydrolysis of a nucleoside triphosphate
Contents
EC 7.4.2.1 ABC-type polar-amino-acid transporter<
EC 7.4.2.2 ABC-type nonpolar-amino-acid transporter<
EC 7.4.2.3 mitochondrial protein-transporting ATPase
Accepted name: ABC-type polar-amino-acid transporter
Reaction: ATP + H2O + polar amino acid-[polar amino acid-binding protein][side 1] = ADP + phosphate + polar amino acid[side 2] + [polar amino acid-binding protein][side 1]
Glossary: nopaline = N-{(1R)-1-carboxy-4-[(diaminomethylene)amino]butyl}-L-glutamate
Other name(s): histidine permease; polar-amino-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, polar-amino-acid-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of polar amino acids. This entry comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
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References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Nikaido, K., Liu, P.Q. and Ferro-Luzzi Ames, G. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubilization, dimerization , and ATPase activity. J. Biol. Chem. 272 (1997) 27745-27752. [PMID: 9346917]
3. Walshaw, D.L., Lowthorpe, S., East, A. and Poole, P.S. Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity. FEBS Lett. 414 (1997) 397-401. [PMID: 9315727]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type nonpolar-amino-acid transporter
Reaction: ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1] = ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
Other name(s): nonpolar-amino-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, nonpolar-amino-acid-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein. This entry comprises enzymes that import Leu, Ile and Val.
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EXPASY,
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References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: mitochondrial protein-transporting ATPase
Reaction: ATP + H2O + mitochondrial-protein[side 1] = ADP + phosphate + mitochondrial-protein[side 2]
Systematic name: ATP phosphohydrolase (mitochondrial protein-importing)
Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex. TIM is the protein transport machinery of the mitochondrial inner membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.
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BRENDA,
EXPASY,
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References:
1. Bomer, U., Meijer, M., Maarse, A.C., Honlinger, A., Dekker, P.J., Pfanner, N. and Rassow, J. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane. EMBO J. 16 (1997) 2205-2216. [PMID: 9171336]
2. Berthold, J., Bauer, M.F., Schneider, H.C., Klaus, C., Dietmeier, K., Neupert, W. and Brunner, M. The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP-driving system. Cell 81 (1995) 1085-1093. [PMID: 7600576]
3. Voos, W., Martin, H., Krimmer, T. and Pfanner, N. Mechanisms of protein translocation into mitochondria. Biochim. Biophys. Acta 1422 (1999) 235-254. [PMID: 10548718]
Accepted name: chloroplast protein-transporting ATPase
Reaction: ATP + H2O + chloroplast-protein[side 1] = ADP + phosphate + chloroplast-protein[side 2]
Systematic name: ATP phosphohydrolase (chloroplast protein-importing)
Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).
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BRENDA,
EXPASY,
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Metacyc,
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References:
1. Cline, K., Ettinger, N.F. and Theg, S.M. Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J. Biol. Chem. 267 (1992) 2688-2696. [PMID: 1733965]
2. Nakai, M., Goto, A., Nohara, T., Sugito, D. and Endo, T. Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J. Biol. Chem. 269 (1994) 31338-33341. [PMID: 7989297]
3. Scott, S.V. and Theg, S.M. A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implications. J. Cell Biol. 132 (1996) 63-75. [PMID: 8567731]
Accepted name: bacterial ABC-type protein transporter
Reaction: ATP + H2O + protein[side 1] = ADP + phosphate + protein[side 2]
Other name(s): PrtDEF (gene names); hasDEF (gene names); peptide-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, peptide-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include α-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
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EXPASY,
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MetaCyc
References:
1. Letoffe, S., Delepelaire, P. and Wandersman, C. Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli α-haemolysin. EMBO J. 9 (1990) 1375-1382. [PMID: 2184029]
2. Klein, C. and Entian, K.D. Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633. Appl. Environ. Microbiol. 60 (1994) 2793-2801. [PMID: 8085823]
3. Binet, R., Létoffé, S., Ghigo, J.M., Delepaire, P. and Wanderman, C. Protein secretion by Gram-negative bacterial ABC exporters - a review. Gene 192 (1997) 7-11. [PMID: 9224868]
Accepted name: ABC-type oligopeptide transporter
Reaction: ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1] = ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
Other name(s): oligopeptide permease; OppBCDF; oligopeptide ABC transporter; oligopeptide-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, oligopeptide-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of oligopeptides of varying nature. The binding protein determines the specificity of the system. cf. EC 7.4.2.9, ABC-type dipeptide transporter.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
3. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
4. Pearce, S.R., Mimmack, M.L., Gallagher, M.P., Gileadi, U., Hyde, S.C. and Higgins, C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 6 (1992) 47-57. [PMID: 1738314]
Accepted name: ABC-type α-factor-pheromone transporter
Reaction: ATP + H2O + α-factor[side 1] = ADP + phosphate + α-factor[side 2]
Other name(s): α-factor-transporting ATPase; α-factor-pheromone transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, α-factor-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports the α-factor sex pheromone.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Michaelis, S. STE6, the yeast α-factor exporter. Semin. Cell Biol. 4 (1993) 17-27. [PMID: 8095825]
2. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: protein-secreting ATPase
Reaction: ATP + H2O + cellular protein[side 1] = ADP + phosphate + cellular protein[side 2]
Systematic name: ATP phosphohydrolase (protein-secreting)
Comments: A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. There are several families of enzymes included here, e.g. ATP-hydrolysing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.
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References:
1. Saier, M.H., Jr. , Tam. R., Reizer, A. and Reizer, J. Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol. Microbiol. 11 (1994) 841-847. [PMID: 8022262]
2. Mecsas, J. and Strauss, E.J. Molecular mechanisms of bacterial virulence: type III secretion and pathogenicity islands. Emerg. Infect. Diseases. 2 (1996) 270-288. [PMID: 8969244]
3. Thomas, J.D., Reeves, P.J. and Salmond, G.P. The general secretion pathway of Erwinia carotovora subsp. carotovora: analysis of the membrane topology of OutC and OutF. Microbiology 143 (1997) 713-720. [PMID: 9084158]
4. Baker, B., Zambryski, P., Staskawicz, B. and Dinesh-Kumar, S.P. Signaling in plant-microbe interactions. Science 276 (1997) 726-733. [PMID: 9115193]
5. Martinez, A., Ostrovsky, P. and Nunn, D.N. Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion. Mol. Microbiol. 28 (1998) 1235-1246. [PMID: 9680212]
6. Schuch, R. and Maurelli, A.T. The mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasin translocation. Infect. Immun. 67 (1999) 1982-1991. [PMID: 10085046]
Accepted name: ABC-type dipeptide transporter
Reaction: ATP + H2O + a dipeptide-[dipeptide-binding protein][side 1] = ADP + phosphate + a dipeptide[side 2] + [dipeptide-binding protein][side 1]
Other name(s): dipeptide transporting ATPase; dipeptide ABC transporter; dppBCDF (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, dipeptide-transporting)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the uptake of di- and tripeptides. The enzyme from Pseudomonas aeruginosa can interact with five different substrate binding proteins.
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EXPASY,
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References:
1. Abouhamad, W.N., Manson, M., Gibson, M.M. and Higgins, C.F. Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein. Mol. Microbiol. 5 (1991) 1035-1047. [PMID: 1956284]
2. Sanz, Y., Lanfermeijer, F.C., Renault, P., Bolotin, A., Konings, W.N. and Poolman, B. Genetic and functional characterization of dpp genes encoding a dipeptide transport system in Lactococcus lactis. Arch. Microbiol. 175 (2001) 334-343. [PMID: 11409543]
3. Li, X., Zhuo, W., Yu, J., Ge, J., Gu, J., Feng, Y., Yang, M., Wang, L. and Wang, N. Structure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron-sulfur cluster-binding domain. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 256-265. [PMID: 23385461]
4. Pletzer, D., Lafon, C., Braun, Y., Kohler, T., Page, M.G., Mourez, M. and Weingart, H. High-throughput screening of dipeptide utilization mediated by the ABC transporter DppBCDF and its substrate-binding proteins DppA1-A5 in Pseudomonas aeruginosa. PLoS One 9 (2014) e111311. [PMID: 25338022]
Accepted name: ABC-type glutathione transporter
Reaction: ATP + H2O + glutathione-[glutathione-binding protein][side 1] = ADP + phosphate + glutathione[side 2] + [glutathione-binding protein][side 1]
Other name(s): glutathione transporting ATPase; glutathione ABC transporter; gsiACD (gene names)
Systematic name: ATP phosphohydrolase (ABC-type,glutathione-importing)
Comments: A prokaryotic ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli is a heterotrimeric complex that interacts with an extracytoplasmic substrate binding protein to mediate the uptake of glutathione.
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BRENDA,
EXPASY,
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MetaCyc,
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References:
1. Suzuki, H., Koyanagi, T., Izuka, S., Onishi, A. and Kumagai, H. The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J. Bacteriol. 187 (2005) 5861-5867. [PMID: 16109926]
2. Moussatova, A., Kandt, C., O'Mara, M.L. and Tieleman, D.P. ATP-binding cassette transporters in Escherichia coli. Biochim. Biophys. Acta 1778 (2008) 1757-1771. [PMID: 18634750]
Accepted name: ABC-type methionine transporter
Reaction: (1) ATP + H2O + L-methionine-[methionine-binding protein][side 1] = ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
Other name(s): methionine transporting ATPase; methionine ABC transporter; metNIQ (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, methionine-importing)
Comments: ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and functions to import methionine. The enzyme from Escherichia coli K-12 mediates the high affinity transport of both L- and D-methionine, as well as methionine-S-oxide and N-acetyl-DL-methionine.
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EXPASY,
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References:
1. Merlin, C., Gardiner, G., Durand, S. and Masters, M. The Escherichia coli metD locus encodes an ABC transporter which includes Abc (MetN), YaeE (MetI), and YaeC (MetQ). J. Bacteriol. 184 (2002) 5513-5517. [PMID: 12218041]
2. Zhang, Z., Feige, J.N., Chang, A.B., Anderson, I.J., Brodianski, V.M., Vitreschak, A.G., Gelfand, M.S. and Saier, M.H., Jr. A transporter of Escherichia coli specific for L- and D-methionine is the prototype for a new family within the ABC superfamily. Arch. Microbiol. 180 (2003) 88-100. [PMID: 12819857]
3. Moussatova, A., Kandt, C., O'Mara, M.L. and Tieleman, D.P. ATP-binding cassette transporters in Escherichia coli. Biochim. Biophys. Acta 1778 (2008) 1757-1771. [PMID: 18634750]
Accepted name: ABC-type cystine transporter
Reaction: (1) ATP + H2O + L-cystine-[cystine-binding protein][side 1] = ADP + phosphate + L-cystine[side 2] + [cystine-binding protein][side 1]
Other name(s): cystine transporting ATPase; cystine ABC transporter
Systematic name: ATP phosphohydrolase (ABC-type, cystine-importing)
Comments: ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity import of trace cystine. The enzyme from Escherichia coli K-12 can import both isomers of cystine and a variety of related molecules including djenkolate, lanthionine, diaminopimelate and homocystine.
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References:
1. Berger, E.A. and Heppel, L.A. A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli. J. Biol. Chem 247 (1972) 7684-7694. [PMID: 4564569]
2. Chonoles Imlay, K.R., Korshunov, S. and Imlay, J.A. Physiological roles and adverse effects of the two cystine importers of Escherichia coli. J. Bacteriol. 197 (2015) 3629-3644. [PMID: 26350134]
Accepted name: ABC-type tyrosine transporter
Reaction: ATP + H2O + L-tyrosinyl-[tyrosine-binding protein][side 1] = ADP + phosphate + L-tyrosine[side 2] + [tyrosine-binding protein][side 1]
Systematic name: ATP phosphohydrolase (ABC-type, L-tyrosine-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in Clostridioides, interacts with an extracytoplasmic substrate binding lipoprotein and mediates the import of L-tyrosine. L-phenylalanine is also tranported however with lower efficiency.
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References:
1. Steglich, M., Hofmann, J.D., Helmecke, J., Sikorski, J., Sproer, C., Riedel, T., Bunk, B., Overmann, J., Neumann-Schaal, M. and Nubel, U. Convergent loss of ABC transporter genes from Clostridioides difficile genomes Is associated with impaired tyrosine uptake and p-cresol production. Front Microbiol 9 (2018) 901. [PMID: 29867812]
Accepted name: ABC-type antigen peptide transporter
Reaction: ATP + H2O + antigen peptide[side 1] = ADP + phosphate + antigen peptide[side 2]
Other name(s): TAP1 (gene name); TAP2 (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, antigen peptide-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. This entry describes vertebrate transporters involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with major histocompatibility complex (MHC) class I molecules. The substrates are generated mainly from degradation of cytosolic proteins by the proteasome.
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EXPASY,
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References:
1. Bahram, S., Arnold, D., Bresnahan, M., Strominger, J.L. and Spies, T. Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region. Proc. Natl. Acad. Sci. USA 88 (1991) 10094-10098. [PMID: 1946428]
2. Momburg, F., Roelse, J., Howard, J.C., Butcher, G.W., Hammerling, G.J. and Neefjes, J.J. Selectivity of MHC-encoded peptide transporters from human, mouse and rat. Nature 367 (1994) 648-651. [PMID: 8107849]
3. Nijenhuis, M. and Hammerling, G.J. Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site. J. Immunol. 157 (1996) 5467-5477. [PMID: 8955196]
Contents
EC 7.5.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.5.2.1 ABC-type maltose transporter
Accepted name: ABC-type maltose transporter
Reaction: ATP + H2O + maltose-[maltose-binding protein][side 1] = ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Other name(s): maltose ABC transporter; maltose-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, maltose-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of maltose and maltose oligosaccharides.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [PMID: 1282354]
2. Dassa, E. and Muir, S. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol. Microbiol. 7 (1993) 29-38. [PMID: 8437518]
3. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type oligosaccharide transporter
Reaction: ATP + H2O + oligosaccharide-[oligosaccharide-binding protein][side 1] = ADP + phosphate + oligosaccharide[side 2] + [oligosaccharide-binding protein][side 1]
Other name(s): oligosaccharide-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, oligosaccharide-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of lactose, melibiose and raffinose.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [PMID: 1282354]
2. Williams, S.G., Greenwood, J.A. and Jones, C.W. Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and β-galactosidase in Agrobacterium radiobacter. Mol. Microbiol. 6 (1992) 1755-1768. [PMID: 1630315]
3. Tam, R. and Saier, M.H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57 (1993) 320-346. [PMID: 8336670]
4. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
5. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type β-glucan transporter
Reaction: ATP + H2O + β-glucan[side 1] = ADP + phosphate + β-glucan[side 2]
Other name(s): β-glucan-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, β-glucan-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. An enzyme found in Gram-negative bacteria that exports β-glucans.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [PMID: 8302219]
2. Becker, A., Kuster, H., Niehaus, K. and Puhler, A. Extension of the Rhizobium meliloti succinoglycan biosynthesis gene cluster: identification of the exsA gene encoding an ABC transporter protein, and the exsB gene which probably codes for a regulator of succinoglycan biosynthesis. Mol. Gen. Genet. 249 (1995) 487-497. [PMID: 8544814]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type teichoic-acid transporter
Reaction: ATP + H2O + teichoic acid[side 1] = ADP + phosphate + teichoic acid[side 2]
Other name(s): teichoic-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, teichoic-acid-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-positive bacteria that exports teichoic acid.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [PMID: 8302219]
2. Lazarevic, V. and Karamoto, D. The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids. Mol. Microbiol. 16 (1995) 345-355. [PMID: 7565096]
3. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [PMID: 9274022]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type lipopolysaccharide transporter
Reaction: ATP + H2O + lipopolysaccharide[side 1] = ADP + phosphate + lipopolysaccharide[side 2]
Other name(s): lptB (gene name); lipopolysaccharide transport system; lipopolysaccharide-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, lipopolysaccharide-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzyme, characterized from the bacterium Escherichia coli, functions as part of the lipopolysaccharide (LPS) export system, a seven protein system that translocates LPS from the inner- to the outer membrane. The ATPase activity in this system is implicated in releasing LPS from the inner membrane.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Sperandeo, P., Cescutti, R., Villa, R., Di Benedetto, C., Candia, D., Deho, G. and Polissi, A. Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli. J. Bacteriol. 189 (2007) 244-253. [PMID: 17056748]
2. Ruiz, N., Gronenberg, L.S., Kahne, D. and Silhavy, T.J. Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli. Proc. Natl Acad. Sci. USA 105 (2008) 5537-5542. [PMID: 18375759]
3. Narita, S. and Tokuda, H. Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides. FEBS Lett. 583 (2009) 2160-2164. [PMID: 19500581]
4. Tran, A.X., Dong, C. and Whitfield, C. Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli. J. Biol. Chem 285 (2010) 33529-33539. [PMID: 20720015]
5. Okuda, S., Freinkman, E. and Kahne, D. Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli. Science 338 (2012) 1214-1217. [PMID: 23138981]
6. Chng, S.S., Gronenberg, L.S. and Kahne, D. Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex. Biochemistry 49 (2010) 4565-4567. [PMID: 20446753]
Accepted name: ABC-type lipid A-core oligosaccharide transporter
Reaction: ATP + H2O + lipid A-core oligosaccharide[side 1] = ADP + phosphate + lipid A-core oligosaccharide[side 2]
Other name(s): MsbA; lipid flippase; ATP-dependent lipid A-core flippase
Systematic name: ATP phosphohydrolase (ABC-type, lipid A-core oligosaccharide-translocating)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, best characterized from the bacterium Escherichia coli, is located in the inner membrane and mediates the movement of lipid A attached to the core oligosaccharide from the cytoplasm to the periplasmic side of the inner membrane, an important step in the lipopolysaccharide biosynthetic pathway. Not to be confused with EC 7.5.2.5, ABC-type lipopolysaccharide
transporter (LptB), which is implicated in the translocation of LPS from the inner membrane to the outer membrane and acts later in the process.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
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CAS registry number:
References:
1. Karow, M. and Georgopoulos, C. The essential Escherichia coli msbA gene, a multicopy suppressor of null mutations in the htrB gene, is related to the universally conserved family of ATP-dependent translocators. Mol. Microbiol. 7 (1993) 69-79. [PMID: 8094880]
2. Zhou, Z., White, K.A., Polissi, A., Georgopoulos, C. and Raetz, C.R. Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis. J. Biol. Chem 273 (1998) 12466-12475. [PMID: 9575204]
3. Singh, H., Velamakanni, S., Deery, M.J., Howard, J., Wei, S.L. and van Veen, H.W. ATP-dependent substrate transport by the ABC transporter MsbA is proton-coupled. Nat Commun 7 (2016) 12387. [PMID: 27499013]
Accepted name: ABC-type D-ribose transporter
Reaction: ATP + H2O + D-ribose-[ribose-binding protein][side 1] = ADP + phosphate + D-ribose[side 2] + [ribose-binding protein][side 1]
Other name(s): D-ribose transporting ATPase; D-ribose ABC transporter; rbsACB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-ribose-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-ribose.
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BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Bell, A.W., Buckel, S.D., Groarke, J.M., Hope, J.N., Kingsley, D.H. and Hermodson, M.A. The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12. J. Biol. Chem 261 (1986) 7652-7658. [PMID: 3011793]
2. Clifton, M.C., Simon, M.J., Erramilli, S.K., Zhang, H., Zaitseva, J., Hermodson, M.A. and Stauffacher, C.V. In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes. J. Biol. Chem 290 (2015) 5555-5565. [PMID: 25533465]
Accepted name: ABC-type D-allose transporter
Reaction: ATP + H2O + D-allose-[allose-binding protein][side 1] = ADP + phosphate + D-allose[side 2] + [allose-binding protein][side 1]
Other name(s): D-allose transporting ATPase; D-allose ABC transporter; alsBAC (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-allose-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-allose, which can be used by the bacterium as a sole carbon source.
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BRENDA,
EXPASY,
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CAS registry number:
References:
1. Kim, C., Song, S. and Park, C. The D-allose operon of Escherichia coli K-12. J. Bacteriol. 179 (1997) 7631-7637. [PMID: 9401019]
Accepted name: ABC-type D-galactofuranose transporter
Reaction: ATP + H2O + D-galactofuranose-[galactofuranose-binding protein][side 1] = ADP + phosphate + D-galactofuranose[side 2] + [galactofuranose-binding protein][side 1]
Other name(s): D-galactofuranose transporting ATPase; D-galactofuranose ABC transporter
Systematic name: ATP phosphohydrolase (ABC-type, D-galactofuranose-transporting)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichai coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of D-galactofuranose. The periplasmic binding protein exhibits selective binding of D-galactofuranose over D-galactopyranose.
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EXPASY,
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References:
1. Horler, R.S., Muller, A., Williamson, D.C., Potts, J.R., Wilson, K.S. and Thomas, G.H. Furanose-specific sugar transport: characterization of a bacterial galactofuranose-binding protein. J. Biol. Chem 284 (2009) 31156-31163. [PMID: 19744923]
Accepted name: ABC-type D-xylose transporter
Reaction: ATP + H2O + D-xylose-[xylose-binding protein][side 1] = ADP + phosphate + D-xylose[side 2] + [xylose-binding protein][side 1]
Other name(s): D-xylose transporting ATPase; D-xylose ABC transporter; xylFGH (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-xylose-transporting)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-xylose.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Song, S. and Park, C. Organization and regulation of the D-xylose operons in Escherichia coli K-12: XylR acts as a transcriptional activator. J. Bacteriol. 179 (1997) 7025-7032. [PMID: 9371449]
2. Linton, K.J. and Higgins, C.F. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28 (1998) 5-13. [PMID: 9593292]
Accepted name: ABC-type D-galactose transporter
Reaction: ATP + H2O + D-galactose-[galactose-binding protein][side 1] = ADP + phosphate + D-galactose[side 2] + [galactose-binding protein][side 1]
Other name(s): D-galactose transporting ATPase; D-galactose ABC transporter; mglBAC (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-galactose-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme, best characterized from Escherichia coli where it interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of D-galactose and methyl-β-D-galactoside.
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BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Hogg, R.W., Voelker, C. and Von Carlowitz, I. Nucleotide sequence and analysis of the mgl operon of Escherichia coli K12. Mol. Gen. Genet. 229 (1991) 453-459. [PMID: 1719366]
Accepted name: ABC-type L-arabinose transporter
Reaction: ATP + H2O + L-arabinose-[arabinose-binding protein][side 1] = ADP + phosphate + L-arabinose[side 2] + [arabinose-binding protein][side 1]
Other name(s): L-arabinose transporting ATPase; L-arabinose ABC transporter; araFGH (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, L-arabinose-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity uptake of L-arabinose.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Scripture, J.B., Voelker, C., Miller, S., O'Donnell, R.T., Polgar, L., Rade, J., Horazdovsky, B.F. and Hogg, R.W. High-affinity L-arabinose transport operon. Nucleotide sequence and analysis of gene products. J. Mol. Biol. 197 (1987) 37-46. [PMID: 2445996]
2. Horazdovsky, B.F. and Hogg, R.W. Genetic reconstitution of the high-affinity L-arabinose transport system. J. Bacteriol. 171 (1989) 3053-3059. [PMID: 2656640]
Accepted name: ABC-type D-xylose/L-arabinose transporter
Reaction: (1) ATP + H2O + D-xylose-[xylose-binding protein][side 1] = ADP + phosphate + D-xylose[side 2] + [xylose-binding protein][side 1]
Systematic name: ATP phosphohydrolase (ABC-type, D-xylose/L-arabinose-importing)
Comments: ATP-binding cassette (ABC) type transporter with a 10-transmembrane-spanning (TMD) subunit and a single nucleotide binding domain. The enzyme from the archaeon Sulfolobus acidocaldarius interacts with an extracytoplasmic sugar-binding protein and mediates the uptake of of D-xylose and L-arabinose (cf. EC 7.5.2.10, ABC-type D-xylose transporter and EC 7.5.2.12, ABC-type L-arabinose transporter).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Wagner, M., Shen, L., Albersmeier, A., van der Kolk, N., Kim, S., Cha, J., Braesen, C., Kalinowski, J., Siebers, B. and Albers, S.-V. Sulfolobus acidocaldarius transports pentoses via a carbohydrate uptake transporter 2 (CUT2)-type ABC transporter and metabolizes them through the aldolase-independent Weimberg pathway. Appl. Environ. Microbiol. 84 (2018) e01273-17. [PMID: 29150511]
Accepted name: ABC-type homopolymeric O-antigen exporter
Reaction: ATP + a lipid-linked O antigen[cytosol] + H2O = ADP + phosphate + a lipid-linked O antigen[periplasm]
Other name(s): wzm (gene name); wzt (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, homopolymeric O-antigen exporting)
Comments: Unlike heteropolymeric O antigens, which are polymerized in the periplasm by EC 2.4.99.27, O antigen polymerase Wzy, homopolymeric O antigens are polymerized inside the cytoplasm by a progressive transfer of sugar monomers to a growing chain attached to a polyprenyl diphosphate membrane anchor. When the chain reaches its full length it is transported across the cytoplasmic membrane by this ABC-type transporter, which consists of an ATP-binding subunit (Wzt) and an integral membrane protein (Wzm). Wzm proteins are poorly conserved in their primary sequence. Once in the periplasm, the O antigen is ligated to the lipid A-core complex by EC 2.4.99.26, O-antigen ligase.
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BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number: 9028-04-0
References:
1. Kido, N., Torgov, V.I., Sugiyama, T., Uchiya, K., Sugihara, H., Komatsu, T., Kato, N. and Jann, K. Expression of the O9 polysaccharide of Escherichia coli: sequencing of the E. coli O9 rfb gene cluster, characterization of mannosyl transferases, and evidence for an ATP-binding cassette transport system. J. Bacteriol. 177 (1995) 2178-2187. [PMID: 7536735]
2. Rocchetta, H.L. and Lam, J.S. Identification and functional characterization of an ABC transport system involved in polysaccharide export of A-band lipopolysaccharide in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 4713-4724. [PMID: 9244257]
3. Cuthbertson, L., Powers, J. and Whitfield, C. The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a. J. Biol. Chem. 280 (2005) 30310-30319. [PMID: 15980069]
4. Cuthbertson, L., Kimber, M.S. and Whitfield, C. Substrate binding by a bacterial ABC transporter involved in polysaccharide export. Proc. Natl. Acad. Sci. USA 104 (2007) 19529-19534. [PMID: 18032609]
5. Mann, E., Mallette, E., Clarke, B.R., Kimber, M.S. and Whitfield, C. The Klebsiella pneumoniae O12 ATP-binding cassette (ABC) transporter recognizes the terminal residue of its O-antigen polysaccharide substrate. J. Biol. Chem. 291 (2016) 9748-9761. [PMID: 26934919]
6. Mann, E., Kelly, S.D., Al-Abdul-Wahid, M.S., Clarke, B.R., Ovchinnikova, O.G., Liu, B. and Whitfield, C. Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen from Escherichia coli O9a. J. Biol. Chem. 294 (2019) 14978-14990. [PMID: 31416837]
EC 7.6.2 Linked to the hydrolysis of a nucleoside triphosphate
Contents
EC 7.6.2.1 P-type phospholipid transporter
Accepted name: P-type phospholipid transporter
Reaction: ATP + H2O + phospholipid[side 1] = ADP + phosphate + phospholipid[side 2]
Other name(s): Mg2+-ATPase (ambiguous); flippase (ambiguous); aminophospholipid-transporting ATPase (ambiguous); phospholipid-translocating ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (P-type, phospholipid-flipping)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme moves phospholipids such as phosphatidylcholine, phosphatidylserine, and phosphatidylethanolamine from one membrane face to the other (‘flippase’).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
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CAS registry number:
References:
1. Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823-832. [PMID: 8136700]
2. Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95-102. [PMID: 8839453]
3. Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429-10434. [PMID: 9099684]
4. Auland, M.E., Roufogalis, B.D., Devaux, P.F. and Zachowski, A. Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes. Proc. Natl. Acad. Sci. USA 91 (1994) 10938-10942. [PMID: 7971987]
5. Alder-Baerens, N., Lisman, Q., Luong, L., Pomorski, T. and Holthuis, J.C. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17 (2006) 1632-1642. [PMID: 16452632]
6. Lopez-Marques, R.L., Poulsen, L.R., Hanisch, S., Meffert, K., Buch-Pedersen, M.J., Jakobsen, M.K., Pomorski, T.G. and Palmgren, M.G. Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA α-subunit. Mol. Biol. Cell 21 (2010) 791-801. [PMID: 20053675]
Accepted name: ABC-type xenobiotic transporter
Reaction: ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
Other name(s): xenobiotic-transporting ATPase; multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting)
Systematic name: ATP phosphohydrolase (ABC-type, xenobiotic-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them also transport glutathione—drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some ‘flippase’ activity (redundant, but not identical, to EC 7.6.2.1, P-type phospholipid transporter).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Bellamy, W.T. P-glycoproteins and multidrug resistance. Annu. Rev. Pharmacol. Toxicol. 36 (1996) 161-183. [PMID: 8725386]
2. Frijters, C.M., Ottenhoff, R., Van Wijland, M.J., Van Nieuwkerk, C., Groen, A.K. and Oude-Elferink, R.P. Influence of bile salts on hepatic mdr2 P-glycoprotein expression. Adv. Enzyme Regul. 36 (1996) 351-363. [PMID: 8869755]
3. Keppler, D., König, J. and Buchler, M. The canalicular multidrug resistance protein, cMRP/MRP2, a novel conjugate export pump expressed in the apical membrane of hepatocytes. Adv. Enzyme Regul. 37 (1997) 321-333. [PMID: 9381978]
4. Loe, D.W., Deeley, R.G. and Cole, S.P. Characterization of vincristine transport by the Mr 190,000 multidrug resistance protein (MRP): evidence for cotransport with reduced glutathione. Cancer Res. 58 (1998) 5130-5136. [PMID: 9823323]
5. van Veen, H.W. and Konings, W.N. The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta 1365 (1998) 31-36. [PMID: 9693718]
6. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
7. Prasad, R., De Wergifosse, P., Goffeau, A. and Balzi, E. Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals. Curr. Genet. 27 (1995) 320-329. [PMID: 7614555]
8. Nagao, K., Taguchi, Y., Arioka, M., Kadokura, H., Takatsuki, A., Yoda, K. and Yamasaki, M. bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily. J. Bacteriol. 177 (1995) 1536-1543. [PMID: 7883711]
9. Mahé, Y., Lemoine, Y. and Kuchler, K. The ATP-binding cassette transporters Pdr5 and Snq2 of Saccharomyces cerevisiae can mediate transport of steroids in vivo. J. Biol. Chem. 271 (1996) 25167-25172. [PMID: 8810273]
Accepted name: ABC-type glutathione-S-conjugate transporter
Reaction: ATP + H2O + glutathione-S-conjugate[side 1] = ADP + phosphate + glutathione-S-conjugate[side 2]
Other name(s): multidrug resistance-associated protein 1; glutathione-S-conjugate-translocating ATPase; MRP; MRP1; ABCC1 (gene name); YBT1 (gene name); YCF1 (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, glutathione-S-conjugate-exporting)
Comments: A eukaryotic ATP-binding cassette (ABC) type transporter that mediates the transport of glutathione-S-conjugates. The mammalian enzyme, which also transports some glucuronides, exports the substrates out of the cell, while plant and fungal transporters export them into the vacuole. Over-expression confers resistance to anticancer drugs by their efficient exportation in glutathione-S-conjugate form.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
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CAS registry number:
References:
1. Zaman, G.J., Flens, M.J., van Leusden, M.R., de Haas, M., Mulder, H.S., Lankelma, J., Pinedo, H.M., Scheper, R.J., Baas, F., Broxterman, H.J. and et al. The human multidrug resistance-associated protein MRP is a plasma membrane drug-efflux pump. Proc. Natl Acad. Sci. USA 91 (1994) 8822-8826. [PMID: 7916458]
2. Lautier, D., Canitrot, Y., Deeley, R.G. and Cole, S.P. Multidrug resistance mediated by the multidrug resistance protein (MRP) gene. Biochem. Pharmacol. 52 (1996) 967-977. [PMID: 8831715]
3. Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509-6517. [PMID: 8626454]
4. Lu, Y.P., Li, Z.S. and Rea, P.A. AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: isolation and functional definition of a plant ATP-binding cassette transporter gene. Proc. Natl Acad. Sci. USA 94 (1997) 8243-8248. [PMID: 9223346]
5. Cole, S.P. Multidrug resistance protein 1 (MRP1, ABCC1), a "multitasking" ATP-binding cassette (ABC) transporter. J. Biol. Chem 289 (2014) 30880-30888. [PMID: 25281745]
6. Cordente, A.G., Capone, D.L. and Curtin, C.D. Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one. Appl. Microbiol. Biotechnol. 99 (2015) 9709-9722. [PMID: 26227410]
Accepted name: ABC-type fatty-acyl-CoA transporter
Reaction: ATP + H2O + fatty acyl CoA[side 1] = ADP + phosphate + fatty acyl CoA[side 2]
Other name(s): fatty-acyl-CoA-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, fatty-acyl-CoA-transporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB,
CAS registry number:
References:
1. Kamijo, K., Taketani, S., Yokota, S., Osumi, T. and Hashimoto, T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glcoprotein)-related ATP-binding protein superfamily. J. Biol. Chem. 265 (1990) 4534-4540. [PMID: 1968461]
2. Hettema, E.H., van Roermund, C.W.T., Distel, B. , van den Berg. M., Vilela, C., Rodrigues-Posada, C., Wanders, R.J.A. and Tabak, H.F. The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. EMBO J. 15 (1996) 3813-3822. [PMID: 8670886]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type heme transporter
Reaction: ATP + H2O + heme[side 1] = ADP + phosphate + heme[side 2]
Other name(s): heme-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, heme-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzyme has been described from Gram-negative bacteria and green plants.
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BRENDA,
EXPASY,
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Metacyc,
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CAS registry number:
References:
1. Ramseier, T.M., Winteler, H.V. and Hennecke, H. Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes. J. Biol. Chem. 266 (1991) 7793-7803. [PMID: 1850420]
2. Jekabsons, W. and Schuster, W. orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria. Mol. Gen. Genet. 246 (1995) 166-173. [PMID: 7862087]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type guanine transporter
Reaction: ATP + H2O + guanine[side 1] = ADP + phosphate + guanine[side 2]
Other name(s): guanine-transporting ATPase; white (gene name); brown (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, guanine-importing)
Comments: An ATP-binding cassette (ABC) type transporter found in insects that transports guanine and other purines into pigment granules in the eye, where they are converted to pteridine pigments. The transporter is a hererodimer composed of two different peptides, each containing one membrane-spanning and one cytoplasmic ATP-binding domain. In Drosophila, this transporter is encoded by the white and brown genes.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Sullivan, D.T., Bell, L.A., Paton, D.R. and Sullivan, M.C. Purine transport by malpighian tubules of pteridine-deficient eye color mutants of Drosophila melanogaster. Biochem. Genet. 17 (1979) 565-573. [PMID: 117796]
2. Dreesen, T.D., Johnson, D.H and Henikoff, S. The brown protein of Drosophila melanogaster is similar to the white protein and to components of active transport complexes. Mol. Cell Biol. 8 (1988) 5206-5215. [PMID: 3149712]
3. Tearle, R.G., Belote, J.M., McKeown, M., Baker, B.S. and Howells, A.J. Cloning and characterization of the scarlet gene of Drosophila melanogaster. Genetics 122 (1989) 595-606. [PMID: 2503416]
4. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
5. Mackenzie, S.M., Brooker, M.R., Gill, T.R., Cox, G.B., Howells, A.J. and Ewart, G.D. Mutations in the white gene of Drosophila melanogaster affecting ABC transporters that determine eye colouration. Biochim. Biophys. Acta 1419 (1999) 173-185. [PMID: 10407069]
Accepted name: ABC-type taurine transporter
Reaction: ATP + H2O + taurine-[taurine-binding protein][side 1] = ADP + phosphate + taurine[side 2] + [taurine-binding protein][side 1]
Other name(s): tauABC (gene names); taurine ABC transporter; taurine-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, taurine-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of taurine. In Escherichia coli the enzyme imports a range of sulfonates (including taurine) that can be used as a source of sulfur.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. van der Ploeg, J.R., Weiss, M.A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M.A. and Leisinger, T. Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178 (1996) 5438-5446. [PMID: 8808933]
Accepted name: ABC-type vitamin B12 transporter
Reaction: ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] = ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
Other name(s): BtuCDF; vitamin B12 ABC transporter; vitamin B12-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, vitamin B12-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of cobalamin derivatives.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Friedrich, M.J., de Veaux, L.C. and Kadner, R.J. Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems. J. Bacteriol. 167 (1986) 928-934. [PMID: 3528129]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type quaternary amine transporter
Reaction: ATP + H2O + quaternary amine-[quaternary amine-binding protein][side 1] = ADP + phosphate + quaternary amine[side 2] + [quaternary amine-binding protein][side 1]
Other name(s): glycine betaine ABC transporter; ProVWX; quaternary-amine ABC transporter; quaternary-amine-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, quaternary-amine-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of quaternary amine derivatives.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
PDB
CAS registry number:
References:
1. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
2. Kempf, B., Gade, J. and Bremer, E. Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant. J. Bacteriol. 179 (1997) 6213-6220. [PMID: 9335265]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type glycerol 3-phosphate transporter
Reaction: ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1] = ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
Other name(s): glycerol-3-phosphate ABC transporter; glycerol-3-phosphate-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, sn-glycerol 3-phosphate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of glycerol 3-phosphate and various glycerophosphodiesters.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
2. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
3. Bahl, H., Burchhardt, G. and Wienecke, A. Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes homologous to Escherichia coli genes encoding integral membrane components of binding-protein-dependent transport systems. FEMS Microbiol. Lett. 65 (1991) 83-87. [PMID: 1874408]
Accepted name: ABC-type polyamine transporter
Reaction: ATP + H2O + polyamine-[polyamine-binding protein][side 1] = ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
Other name(s): polyamine ABC transporter; polyamine-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, polyamine-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports putrescine and spermidine. In Escherichia coli the enzyme imports spermidine preferentially.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
Metacyc,
CAS registry number:
References:
1. Kashiwagi, K., Miyamoto, S., Nukui, E., Kobayashi, H. and Igarashi, K. Functions of potA and potD proteins in spermidine - preferential uptake system in Escherichia coli. J. Biol. Chem. 268 (1993) 19358-19363. [PMID: 8366082]
2. Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271-278. [PMID: 7569321]
3. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
Accepted name: ABC-type capsular-polysaccharide transporter
Reaction: ATP + H2O + capsular polysaccharide-[capsular polysaccharide-binding protein][side 1] = ADP + phosphate + capsular polysaccharide[side 2] + [capsular polysaccharide-binding protein][side 1]
Other name(s): capsular-polysaccharide-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, capsular-polysaccharide-exporting)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme that exports capsular polysaccharide in Gram-negative bacteria.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995-1017. [PMID: 8302219]
2. Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685-2699. [PMID: 9274022]
3. Pigeon, R.P. and Silver, R.P. Analysis of the G93E mutant allele of KpsM, the membrane component of an ABC transporter involved in polysialic acid translocation in Escherichia coli K1. FEMS Microbiol. Lett. 156 (1997) 217-222. [PMID: 9513268]
4. Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81-136. [PMID: 9889977]
5. Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
Accepted name: ABC-type autoinducer-2 transporter
Reaction: ATP + H2O + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran-[AI-2-binding protein][side 1] = ADP + phosphate + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran[side 2] + [AI-2-binding protein][side 1]
Glossary: autoinducer-2 = AI-2 = (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran
Other name(s): autoinducer-2 transporting ATPase; autoinducer-2 ABC transporter; LsrACDB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, AI-2 importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the uptake of the signalling molecule (2R,4S)-2-methyl-2,3,3,4-tetrahydoxytetrahydrofuran (also known as autoinducer-2).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Taga, M.E., Semmelhack, J.L. and Bassler, B.L. The LuxS-dependent autoinducer AI-2 controls the expression of an ABC transporter that functions in AI-2 uptake in Salmonella typhimurium. Mol. Microbiol. 42 (2001) 777-793. [PMID: 11722742]
2. Xavier, K.B. and Bassler, B.L. Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli. J. Bacteriol. 187 (2005) 238-248. [PMID: 15601708]
Accepted name: ABC-type aliphatic sulfonate transporter
Reaction: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein][side 1] = ADP + phosphate + aliphatic sulfonate[side 2] + [sulfonate-binding protein][side 1]
Other name(s): aliphatic sulfonate transporting ATPase; alkane sulfonate ABC transporter; aliphatic sulfonate ABC transporter; ssuACB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, aliphatic sulfonate-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli K-12 interacts with an extracytoplasmic substrate binding protein and imports a broad range of aliphatic sulfonates for use as a source of sulfur.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. van Der Ploeg, J.R., Iwanicka-Nowicka, R., Bykowski, T., Hryniewicz, M.M. and Leisinger, T. The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl. J. Biol. Chem 274 (1999) 29358-29365. [PMID: 10506196]
2. Kertesz, M.A. Bacterial transporters for sulfate and organosulfur compounds. Res. Microbiol. 152 (2001) 279-290. [PMID: 11421275]
3. Davidson, A.L., Dassa, E., Orelle, C. and Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72 (2008) 317. [PMID: 18535149]
Accepted name: ABC-type thiamine transporter
Reaction: ATP + H2O + thiamine-[thiamine-binding protein][side 1] = ADP + phosphate + thiamine[side 2] + [thiamine-binding protein][side 1]
Other name(s): thiamin transporting ATPase; thiamine ABC transporter; thiamin ABC transporter; thiamine transporting ATPase; thiBPQ (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, thiamine-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, characterized from the bacterium Salmonella typhimurium, is a heterodimeric complex that interacts with an extracytoplasmic substrate binding protein and functions to import thiamine, thiamine monophosphate and thiamine diphosphate.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Webb, E., Claas, K. and Downs, D. thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium. J. Biol. Chem 273 (1998) 8946-8950. [PMID: 9535878]
Accepted name: ABC-type putrescine transporter
Reaction: ATP + H2O + putrescine-[putrescine-binding protein][side 1] = ADP + phosphate + putrescine[side 2] + [putrescine-binding protein][side 1]
Other name(s): putrescine transporting ATPase; putrescine ABC transporter; potFGHI (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, putrescine-importing)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of putrescine. Differs in specificity from EC 7.6.2.11, ABC-type polyamine transporter.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Pistocchi, R., Kashiwagi, K., Miyamoto, S., Nukui, E., Sadakata, Y., Kobayashi, H. and Igarashi, K. Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome. J. Biol. Chem 268 (1993) 146-152. [PMID: 8416922]
2. Terui, Y., Saroj, S.D., Sakamoto, A., Yoshida, T., Higashi, K., Kurihara, S., Suzuki, H., Toida, T., Kashiwagi, K. and Igarashi, K. Properties of putrescine uptake by PotFGHI and PuuP and their physiological significance in Escherichia coli. Amino Acids 46 (2014) 661-670. [PMID: 23719730]
EC 7.2.2.2 BC-type Cd2+ transporter
EC 7.2.2.3 P-type Na+ transporter
EC 7.2.2.4 ABC-type Na+ transporter<
EC 7.2.2.5 ABC-type Mn2+ transporter
EC 7.2.2.6 P-type K+ transporter
EC 7.2.2.7 ABC-type Fe3+ transporter
EC 7.2.2.8 P-type Cu+ transporter
EC 7.2.2.9 P-type Cu2+ transporter
EC 7.2.2.10 P-type Ca2+ transporter
EC 7.2.2.11 ABC-type Ni2+ transporter
EC 7.2.2.12 P-type Zn2+ transporter
EC 7.2.2.13 Na+/K+-exchanging ATPase
EC 7.2.2.14 P-type Mg2+ transporter
EC 7.2.2.15 P-type Ag+ transporter
EC 7.2.2.16 ABC-type ferric hydroxamate transporter
EC 7.2.2.17 ABC-type ferric enterobactin transporter
EC 7.2.2.18 ABC-type ferric citrate transporter
EC 7.2.2.19 H+/K+-exchanging ATPase
EC 7.2.2.20 ABC-type Zn2+ transporter
EC 7.2.2.21 Cd2+-exporting ATPase
EC 7.2.2.22 P-type Mn2+ transporter
Entries
EC 7.2.3 Linked to the hydrolysis of diphosphate
EC 7.2.4.2 oxaloacetate decarboxylase (Na+ extruding)
EC 7.2.4.3 (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)
EC 7.2.4.4 biotin-dependent malonate decarboxylase
EC 7.2.4.5 glutaconyl-CoA decarboxylase
Entries
EC 7.3 Catalysing the translocation of inorganic anions and their chelates
EC 7.3.2.2 ABC-type phosphonate transporter
EC 7.3.2.3 ABC-type sulfate transporter
EC 7.3.2.4 ABC-type nitrate transporter
EC 7.3.2.5 ABC-type molybdate transporter
EC 7.3.2.6 ABC-type tungstate transporter
EC 7.3.2.7 arsenite-transporting ATPase
Entries
EC 7.4 Catalysing the translocation amino acids and peptides
EC 7.4.2.4 chloroplast protein-transporting ATPase
EC 7.4.2.5 bacterial ABC-type protein transporter
EC 7.4.2.6 ABC-type oligopeptide transporter
EC 7.4.2.7 ABC-type α-factor-pheromone transporter
EC 7.4.2.8 protein-secreting ATPase
EC 7.4.2.9 ABC-type dipeptide transporter
EC 7.4.2.10 ABC-type glutathione transporter
EC 7.4.2.11 ABC-type methionine transporter
EC 7.4.2.12 ABC-type cystine transporter
EC 7.4.2.13 ABC-type tyrosine transporter
EC 7.4.2.14 ABC-type antigen peptide transporter
Entries
(2) ATP + H2O + D-methionine-[methionine-binding protein][side 1] = ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
(2) ATP + H2O + D-cystine-[cystine-binding protein][side 1] = ADP + phosphate + D-cystine[side 2] + [cystine-binding protein][side 1]
EC 7.5 Catalysing the translocation carbohydrates and their derivatives
EC 7.5.2.2 ABC-type oligosaccharide transporter
EC 7.5.2.3 ABC-type β-glucan transporter
EC 7.5.2.4 ABC-type teichoic-acid transporter
EC 7.5.2.5 ABC-type lipopolysaccharide transporter
EC 7.5.2.6 ABC-type lipid A-core oligosaccharide transporter
EC 7.5.2.7 ABC-type D-ribose transporter
EC 7.5.2.8 ABC-type D-allose transporter
EC 7.5.2.9 ABC-type D-galactofuranose transporter
EC 7.5.2.10 ABC-type D-xylose transporter
EC 7.5.2.11 ABC-type D-galactose transporter
EC 7.5.2.12 ABC-type L-arabinose transporter
EC 7.5.2.13 ABC-type D-xylose/L-arabinose transporter
EC 7.5.2.14 ABC-type homopolymeric O-antigen exporter
Entries
(2) ATP + H2O + L-arabinose-[arabinose-binding protein][side 1] = ADP + phosphate + L-arabinose[side 2] + [arabinose-binding protein][side 1]
EC 7.6 Catalysing the translocation of other compounds
EC 7.6.2.2 ABC-type xenobiotic transporter
EC 7.6.2.3 ABC-type glutathione-S-conjugate transporter
EC 7.6.2.4 ABC-type fatty-acyl-CoA transporter
EC 7.6.2.5 ABC-type heme transporter
EC 7.6.2.6 ABC-type guanine transporter
EC 7.6.2.7 ABC-type taurine transporter
EC 7.6.2.8 ABC-type vitamin B12 transporter
EC 7.6.2.9 ABC-type quaternary amine transporter
EC 7.6.2.10 ABC-type glycerol 3-phosphate transporter
EC 7.6.2.11 ABC-type polyamine transporter
EC 7.6.2.12 ABC-type capsular-polysaccharide transporter
EC 7.6.2.13 ABC-type autoinducer-2 transporter
EC 7.6.2.14 ABC-type aliphatic sulfonate transporter
EC 7.6.2.15 ABC-type thiamine transporter
EC 7.6.2.16 ABC-type putrescine transporter
Continued with EC 6
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