EC 2.7.1.1 to EC 2.7.1.50
EC 2.7.1.51 to EC 2.7.1.100
Accepted name: inositol-polyphosphate multikinase
Reaction: (1a) ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
(1b) ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
For diagram, click here
Other name(s): IpK2; IP3/IP4 6-/3-kinase; IP3/IP4 dual-specificity 6-/3-kinase; IpmK; ArgRIII; AtIpk2α; AtIpk2β; inositol polyphosphate 6-/3-/5-kinase
Systematic name: ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase
Comments: This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively [3]. Yeast produce InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158, inositol-pentakisphosphate 2-kinase [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9077-69-4
References:
1. Saiardi, A., Erdjument-Bromage, H., Snowman, A.M., Tempst, P. and Snyder, S.H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9 (1999) 1323-1326. [PMID: 10574768]
2. Odom, A.R., Stahlberg, A., Wente, S.R. and York, J.D. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science 287 (2000) 2026-2029. [PMID: 10720331]
3. Stevenson-Paulik, J., Odom, A.R. and York, J.D. Molecular and biochemical characterization of two plant inositol polyphosphate 6-/3-/5-kinases. J. Biol. Chem. 277 (2002) 42711-42718. [PMID: 12226109]
4. Verbsky, J.W., Chang, S.C., Wilson, M.P., Mochizuki, Y. and Majerus, P.W. The pathway for the production of inositol hexakisphosphate in human cells. J. Biol. Chem. 280 (2005) 1911-1920. [PMID: 15531582]
[EC 2.7.1.152 Transferred entry: now EC 2.7.4.21 inositol-hexakisphosphate kinase. (EC 2.7.1.152 created 2002, deleted 2003)]
Accepted name: phosphatidylinositol-4,5-bisphosphate 3-kinase
Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
For diagram click here.
Other name(s): type I phosphoinositide 3-kinase
Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 3-phosphotransferase
Comments: This enzyme also catalyses the phosphorylation of PtdIns4P to PtdIns(3,4)P2, and of PtdIns to PtdIns3P. Four mammalian isoforms are known to exist.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 103843-30-7
References:
1. Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535-602. [PMID: 11395417]
Accepted name: phosphatidylinositol-4-phosphate 3-kinase
Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
For diagram click here.
Glossary: 1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P2
Other name(s): type II phosphoinositide 3-kinase; C2-domain-containing phosphoinositide 3-kinase; phosphoinositide 3-kinase
Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 3-phosphotransferase
Comments: This enzyme also phosphorylates PtdIns to PtdIns3P. Three mammalian isoforms have been found to date.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 141176-94-5
References:
1. Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535-602. [PMID: 11395417]
[EC 2.7.1.155 Transferred entry: diphosphoinositol-pentakisphosphate kinase. Now EC 2.7.4.24, diphosphoinositol-pentakisphosphate kinase. The enzyme had been incorrectly classified as the reaction involves transfer of a phospho group to another phospho group (EC 2.7.4) rather than to an hydroxy group (EC 2.7.1). (EC 2.7.1.155 created 2003, deleted 2007)]
Accepted name: adenosylcobinamide kinase
Reaction: RTP + adenosylcobinamide = adenosylcobinamide phosphate + RDP
where RTP is either ATP or GTP (for symbol definitions, click here)
For diagram of reaction click here.
Other name(s): CobU; adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; AdoCbi kinase/AdoCbi-phosphate guanylyltransferase
Systematic name: RTP:adenosylcobinamide phosphotransferase
Comments: In Salmonella typhimurium LT2, under anaerobic conditions, CobU (EC 2.7.7.62 and EC 2.7.1.156), CobT (EC 2.4.2.21), CobC (EC 3.1.3.73) and CobS (EC 2.7.8.26) catalyse reactions in the nucleotide loop assembly pathway, which convert adenosylcobinamide (AdoCbi) into adenosylcobalamin (AdoCbl). CobT and CobC are involved in 5,6-dimethylbenzimidazole activation whereby 5,6-dimethylbenzimidazole is converted to its riboside, α-ribazole. The second branch of the nucleotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by Cob U. The final step in adenosylcobalamin biosynthesis is the condensation of AdoCbi-GDP with α-ribazole, which is catalysed by EC 2.7.8.26, adenosylcobinamide-GDP ribazoletransferase (CobS), to yield adenosylcobalamin. CobU is a bifunctional enzyme that has both kinase (EC 2.7.1.156) and guanylyltransferase (EC 2.7.7.62, adenosylcobinamide-phosphate guanylyltransferase) activities. However, both activities are not required at all times. The kinase activity has been proposed to function only when S. typhimurium is assimilating cobinamide whereas the guanylyltransferase activity is required for both assimilation of exogenous cobinamide and for de novo synthesis of adenosylcobalamin [4].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 169592-51-2
References:
1. O'Toole, G.A. and Escalante-Semerena, J.C. Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate. J. Biol. Chem. 270 (1995) 23560-23569. [PMID: 7559521]
2. Thompson, T.B., Thomas, M.G., Escalante-Semerena, J.C. and Rayment, I. Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 Å resolution. Biochemistry 37 (1998) 7686-7695. [PMID: 9601028]
3. Thompson, T.B., Thomas, M.G., Escalante-Semerena, J.C. and Rayment, I. Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase (CobU) complexed with GMP: evidence for a substrate-induced transferase active site. Biochemistry 38 (1999) 12995-13005. [PMID: 10529169]
4. Thomas, M.G., Thompson, T.B., Rayment, I. and Escalante-Semerena, J.C. Analysis of the adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU) enzyme of Salmonella typhimurium LT2. Identification of residue His-46 as the site of guanylylation. J. Biol. Chem. 275 (2000) 27576-27586. [PMID: 10869342]
5. Warren, M.J., Raux, E., Schubert, H.L. and Escalante-Semerena, J.C. The biosynthesis of adenosylcobalamin (vitamin B12). Nat. Prod. Rep. 19 (2002) 390-412. [PMID: 12195810]
Accepted name: N-acetylgalactosamine kinase
Reaction: ATP + N-acetyl-α-D-galactosamine = ADP + N-acetyl-α-D-galactosamine 1-phosphate
Other name(s): GALK2; GK2; GalNAc kinase; N-acetylgalactosamine (GalNAc)-1-phosphate kinase
Systematic name: ATP:N-acetyl-D-galactosamine 1-phosphotransferase
Comments: The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose [2]. Requires Mg2+, Mn2+ or Co2+ for activity, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Pastuszak, I., Drake, R. and Elbein, A.D. Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation. J. Biol. Chem. 271 (1999) 20776-20782. [PMID: 8702831]
2. Pastuszak, I., O'Donnell, J. and Elbein, A.D. Identification of the GalNAc kinase amino acid sequence. J. Biol. Chem. 271 (1996) 23653-23656. [PMID: 8798585]
3. Thoden, J.B. and Holden, H.M. The molecular architecture of human N-acetylgalactosamine kinase. J. Biol. Chem. (2005) 32784-32791 [PMID: 16006554]
Accepted name: inositol-pentakisphosphate 2-kinase
Reaction: ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol hexakisphosphate
Other name(s): IP5 2-kinase; Gsl1p; Ipk1p; Plc1p; inositol polyphosphate kinase; inositol 1,3,4,5,6-pentakisphosphate 2-kinase; Ins(1,3,4,5,6)P5 2-kinase
Systematic name: ATP:1D-myo-inositol 1,3,4,5,6-pentakisphosphate 2-phosphotransferase
Comments: The enzyme can also use Ins(1,4,5,6)P4 [2] and Ins(1,4,5)P3 [3] as substrate. Inositol hexakisphosphate (phytate) accumulates in storage protein bodies during seed development and, when hydrolysed, releases stored nutrients to the developing seedling before the plant is capable of absorbing nutrients from its environment [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. York, J.D., Odom, A.R., Murphy, R., Ives, E.B. and Wente, S.R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285 (1999) 96-100. [PMID: 10390371]
2. Phillippy, B.Q., Ullah, A.H. and Ehrlich, K.C. Purification and some properties of inositol 1,3,4,5,6-Pentakisphosphate 2-kinase from immature soybean seeds. J. Biol. Chem. 269 (1994) 28393-28399. [PMID: 7961779]
3. Ongusaha, P.P., Hughes, P.J., Davey, J. and Michell, R.H. Inositol hexakisphosphate in Schizosaccharomyces pombe: synthesis from Ins(1,4,5)P3 and osmotic regulation. Biochem. J. 335 (1998) 671-679. [PMID: 9794810]
4. Miller, A.L., Suntharalingam, M., Johnson, S.L., Audhya, A., Emr, S.D. and Wente, S.R. Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway. J. Biol. Chem. 279 (2004) 51022-51032. [PMID: 15459192]
5. Stevenson-Paulik, J., Odom, A.R. and York, J.D. Molecular and biochemical characterization of two plant inositol polyphosphate 6-/3-/5-kinases. J. Biol. Chem. 277 (2002) 42711-42718. [PMID: 12226109]
Accepted name: inositol-1,3,4-trisphosphate 5/6-kinase
Reaction: (1) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
(2) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
Other name(s): Ins(1,3,4)P3 5/6-kinase; inositol trisphosphate 5/6-kinase
Systematic name: ATP:1D-myo-inositol 1,3,4-trisphosphate 5-phosphotransferase
Comments: In humans, this enzyme, along with EC 2.7.1.127 (inositol-trisphosphate 3-kinase), EC 2.7.1.140 (inositol-tetrakisphosphate 5-kinase) and EC 2.7.1.158 (inositol pentakisphosphate 2-kinase) is involved in the production of inositol hexakisphosphate (InsP6). InsP6 is involved in many cellular processes, including mRNA export from the nucleus [2]. Yeast do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3 by the actions of EC 2.7.1.151 (inositol-polyphosphate multikinase) and EC 2.7.1.158 (inositol-pentakisphosphate 2-kinase) [2]. The enzymes from animals and plants also have the activity of EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 288307-53-9
References:
1. Wilson, M.P. and Majerus, P.W. Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme. J. Biol. Chem. 271 (1996) 11904-11910. [PMID: 8662638]
2. Verbsky, J.W., Chang, S.C., Wilson, M.P., Mochizuki, Y. and Majerus, P.W. The pathway for the production of inositol hexakisphosphate in human cells. J. Biol. Chem. 280 (2005) 1911-1920. [PMID: 15531582]
Accepted name: 2'-phosphotransferase
Reaction: 2'-phospho-[ligated tRNA] + NAD+ = mature tRNA + ADP-ribose 1",2"-phosphate + nicotinamide
For diagram click here and for mechanism, click here.
Glossary: ADP-ribose = adenosine 5'-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Other name(s): yeast 2'-phosphotransferase; Tpt1; Tpt1p; 2'-phospho-tRNA:NAD+ phosphotransferase
Systematic name: 2'-phospho-[ligated tRNA]:NAD+ phosphotransferase
Comments: Catalyses the final step of tRNA splicing in the yeast Saccharomyces cerevisiae [2]. The reaction takes place in two steps: in the first step, the 2'-phosphate on the RNA substrate is ADP-ribosylated, causing the relase of nicotinamide and the formation of the reaction intermediate, ADP-ribosylated tRNA [6]. In the second step, dephosphorylated (mature) tRNA is formed along with ADP ribose 1",2"-cyclic phosphate. Highly specific for oligonucleotide substrates bearing an internal 2'-phosphate. Oligonucleotides with only a terminal 5'- or 3'-phosphate are not substrates [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 126905-00-8
References:
1. Steiger, M.A., Kierzek, R., Turner, D.H. and Phizicky, E.M. Substrate recognition by a yeast 2'-phosphotransferase involved in tRNA splicing and by its Escherichia coli homolog. Biochemistry 40 (2001) 14098-14105. [PMID: 11705403]
2. Spinelli, S.L., Kierzek, R., Turner, D.H. and Phizicky, E.M. Transient ADP-ribosylation of a 2'-phosphate implicated in its removal from ligated tRNA during splicing in yeast. J. Biol. Chem. 274 (1999) 2637-2644. [PMID: 9915792]
3. Culver, G.M., McCraith, S.M., Consaul, S.A., Stanford, D.R. and Phizicky, E.M. A 2'-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae. J. Biol. Chem. 272 (1997) 13203-13210. [PMID: 9148937]
4. McCraith, S.M. and Phizicky, E.M. An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the splice junction 2'-phosphate from ligated tRNA to an acceptor molecule. J. Biol. Chem. 266 (1991) 11986-11992. [PMID: 2050693]
5. Hu, Q.D., Lu, H., Huo, K., Ying, K., Li, J., Xie, Y., Mao, Y. and Li, Y.Y. A human homolog of the yeast gene encoding tRNA 2'-phosphotransferase: cloning, characterization and complementation analysis. Cell. Mol. Life Sci. 60 (2003) 1725-1732. [PMID: 14504659]
6. Steiger, M.A., Jackman, J.E. and Phizicky, E.M. Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism. RNA 11 (2005) 99-106. [PMID: 15611300]
7. Sawaya, R., Schwer, B. and Shuman, S. Structure-function analysis of the yeast NAD+-dependent tRNA 2'-phosphotransferase Tpt1. RNA 11 (2005) 107-113. [PMID: 15611301]
8. Kato-Murayama, M., Bessho, Y., Shirouzu, M. and Yokoyama, S. Crystal structure of the RNA 2'-phosphotransferase from Aeropyrum pernix K1. J. Mol. Biol. 348 (2005) 295-305. [PMID: 15811369]
Accepted name: CTP-dependent riboflavin kinase
Reaction: CTP + riboflavin = CDP + FMN
Other name(s): Methanocaldococcus jannaschii Mj0056; Mj0056
Systematic name: CTP:riboflavin 5'-phosphotransferase
Comments: This archaeal enzyme differs from EC 2.7.1.26, riboflavin kinase, in using CTP as the donor nucleotide. UTP, but not ATP or GTP, can also act as a phosphate donor but it is at least an order of magnitude less efficient than CTP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ammelburg, M., Hartmann, M.D., Djuranovic, S., Alva, V., Koretke, K.K., Martin, J., Sauer, G., Truffault, V., Zeth, K., Lupas, A.N. and Coles, M. A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels. Structure 15 (2007) 1577-1590. [PMID: 18073108]
Accepted name: N-acetylhexosamine 1-kinase
Reaction: ATP + N-acetyl-D-hexosamine = ADP + N-acetyl-α-D-hexosamine 1-phosphate
Other name(s): NahK; LnpB; N-acetylgalactosamine/N-acetylglucosamine 1-kinase
Systematic name: ATP:N-acetyl-D-hexosamine 1-phosphotransferase
Comments: This enzyme is involved in the lacto-N-biose I/galacto-N-biose degradation pathway in the probiotic bacterium Bifidobacterium longum. Differs from EC 2.7.1.157, N-acetylgalactosamine kinase, as it can phosphorylate both N-acetylgalactosamine and N-acetylglucosamine at similar rates. Also has some activity with N-acetyl-D-mannosamine, D-talose and D-mannose as substrate. ATP can be replaced by GTP or ITP but with decreased enzyme activity. Requires a divalent cation, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Nishimoto, M. and Kitaoka, M. Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum. Appl. Environ. Microbiol. 73 (2007) 6444-6449. [PMID: 17720833]
Accepted name: hygromycin B 4-O-kinase
Reaction: ATP + hygromycin B = ADP + 4-O-phosphohygromycin B
Other name(s): hygromycin-B kinase (ambiguous)
Systematic name: ATP:hygromycin-B 4-O-phosphotransferase
Comments: Phosphorylates the antibiotic hygromycin B. Whereas the enzyme from Streptomyces hygroscopicus (EC 2.7.1.119; hygromycin-B 7"-O-kinase) catalyses the formation of 7"-O-phosphohygromycin B, this enzyme, found in Escherichia coli carrying a plasmid conferring resistance to hygromycin-B, forms 4-O-phosphohygromycin B.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Rao, R.N., Allen, N.E., Hobbs, J.N., Jr., Alborn, W.E., Jr., Kirst, H.A. and Paschal, J.W. Genetic and enzymatic basis of hygromycin B resistance in Escherichia coli. Antimicrob. Agents Chemother. 24 (1983) 689-695. [PMID: 6318654]
Accepted name: O-phosphoseryl-tRNASec kinase
Reaction: ATP + L-seryl-tRNASec = ADP + O-phospho-L-seryl-tRNASec
Other name(s): PSTK; phosphoseryl-tRNA[Ser]Sec kinase; phosphoseryl-tRNASec kinase
Systematic name: ATP:L-seryl-tRNASec O-phosphotransferase
Comments: In archaea and eukarya selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous L-seryl-tRNASec to O-phospho-L-seryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by EC 2.9.1.2 (Sep-tRNA:Sec-tRNA synthase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 91273-83-5
References:
1. Carlson, B.A., Xu, X.M., Kryukov, G.V., Rao, M., Berry, M.J., Gladyshev, V.N. and Hatfield, D.L. Identification and characterization of phosphoseryl-tRNA[Ser]Sec kinase. Proc. Natl. Acad. Sci. USA 101 (2004) 12848-12853. [PMID: 15317934]
2. Sherrer, R.L., O'Donoghue, P. and Soll, D. Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation. Nucleic Acids Res. 36 (2008) 1187-1199. [PMID: 18174226]
3. Khangulov, S.V., Gladyshev, V.N., Dismukes, G.C. and Stadtman, T.C. Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. Biochemistry 37 (1998) 3518-3528. [PMID: 9521673]
Accepted name: glycerate 2-kinase
Reaction: ATP + D-glycerate = ADP + 2-phospho-(R)-glycerate
For diagram of reaction click here.
Other name(s): D-glycerate-2-kinase; glycerate kinase (2-phosphoglycerate forming); ATP:(R)-glycerate 2-phosphotransferase
Systematic name: ATP:D-glycerate 2-phosphotransferase
Comments: A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea [1,2]. In Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assimilation I (serine pathway) [5]. In Escherichia coli the enzyme is involved in D-glucarate/D-galactarate degradation [6]. The enzyme requires a divalent metal ion [1].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Liu, B., Wu, L., Liu, T., Hong, Y., Shen, Y. and Ni, J. A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties. Biotechnol. Lett. 31 (2009) 1937-1941. [PMID: 19690808]
2. Reher, M., Bott, M. and Schonheit, P. Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus. FEMS Microbiol. Lett. 259 (2006) 113-119. [PMID: 16684110]
3. Liu, B., Hong, Y., Wu, L., Li, Z., Ni, J., Sheng, D. and Shen, Y. A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization. Extremophiles 11 (2007) 733-739. [PMID: 17563835]
4. Noh, M., Jung, J.H. and Lee, S.B. Purification and characterization of glycerate kinase from the thermoacidophilic archaeon Thermoplasma acidophilum: an enzyme belonging to the second glycerate kinase family. Biotechnol. Bioprocess Eng. 11 (2006) 344-350.
5. Yoshida, T., Fukuta, K., Mitsunaga, T., Yamada, H. and Izumi, Y. Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2. Eur. J. Biochem. 210 (1992) 849-854. [PMID: 1336459]
6. Hubbard, B.K., Koch, M., Palmer, D.R., Babbitt, P.C. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry 37 (1998) 14369-14375. [PMID: 9772162]
Accepted name: 3-deoxy-D-manno-octulosonic acid kinase
Reaction: α-Kdo-(2→6)-lipid IVA + ATP = 4-O-phospho-α-Kdo-(2→6)-lipid IVA + ADP
Glossary: (KDO)-lipid IVA = α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
(4-O-phospho-KDO)-lipid IVA = 4-O-phospho-α-Kdo-(2→6)-lipid IVA = (3-deoxy-4-O-phosphono-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
Other name(s): kdkA (gene name); Kdo kinase
Systematic name: ATP:(KDO)-lipid IVA 3-deoxy-α-D-manno-oct-2-ulopyranose 4-phosphotransferase
Comments: The enzyme phosphorylates the 4-OH position of KDO in (KDO)-lipid IVA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Brabetz, W., Muller-Loennies, S. and Brade, H. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and kdo kinase (KdkA) of Haemophilus influenzae are both required to complement a waaA knockout mutation of Escherichia coli. J. Biol. Chem. 275 (2000) 34954-34962. [PMID: 10952982]
2. Harper, M., Boyce, J.D., Cox, A.D., St Michael, F., Wilkie, I.W., Blackall, P.J. and Adler, B. Pasteurella multocida expresses two lipopolysaccharide glycoforms simultaneously, but only a single form is required for virulence: identification of two acceptor-specific heptosyl I transferases. Infect. Immun. 75 (2007) 3885-3893. [PMID: 17517879]
3. White, K.A., Kaltashov, I.A., Cotter, R.J. and Raetz, C.R. A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae. J. Biol. Chem. 272 (1997) 16555-16563. [PMID: 9195966]
4. White, K.A., Lin, S., Cotter, R.J. and Raetz, C.R. A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in bacterial virulence. J. Biol. Chem. 274 (1999) 31391-31400. [PMID: 10531340]
Accepted name: D-glycero-β-D-manno-heptose-7-phosphate kinase
Reaction: D-glycero-D-manno-heptose 7-phosphate + ATP = D-glycero-β-D-manno-heptose 1,7-bisphosphate + ADP
Other name(s): heptose 7-phosphate kinase; D-β-D-heptose 7-phosphotransferase; D-β-D-heptose-7-phosphate kinase; HldE1 heptokinase; glycero-manno-heptose 7-phosphate kinase; D-β-D-heptose 7-phosphate kinase/D-β-D-heptose 1-phosphate adenylyltransferase; hldE (gene name); rfaE (gene name)
Systematic name: ATP:D-glycero-β-D-manno-heptose 7-phosphate 1-phosphotransferase
Comments: The bifunctional protein hldE includes D-glycero-β-D-manno-heptose-7-phosphate kinase and D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase activity (cf. EC 2.7.7.70). The enzyme is involved in biosynthesis of ADP-L-glycero-β-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. The enzyme selectively produces D-glycero-β-D-manno-heptose 1,7-bisphosphate [5].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. McArthur, F., Andersson, C.E., Loutet, S., Mowbray, S.L. and Valvano, M.A. Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis. J. Bacteriol. 187 (2005) 5292-5300. [PMID: 16030223]
2. Kneidinger, B., Marolda, C., Graninger, M., Zamyatina, A., McArthur, F., Kosma, P., Valvano, M.A. and Messner, P. Biosynthesis pathway of ADP-L-glycero-β-D-manno-heptose in Escherichia coli. J. Bacteriol. 184 (2002) 363-369. [PMID: 11751812]
3. Valvano, M.A., Messner, P. and Kosma, P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 148 (2002) 1979-1989. [PMID: 12101286]
4. Jin, U.H., Chung, T.W., Lee, Y.C., Ha, S.D. and Kim, C.H. Molecular cloning and functional expression of the rfaE gene required for lipopolysaccharide biosynthesis in Salmonella typhimurium. Glycoconj. J. 18 (2001) 779-787. [PMID: 12441667]
5. Wang, L., Huang, H., Nguyen, H.H., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB). Biochemistry 49 (2010) 1072-1081. [PMID: 20050615]
Accepted name: D-glycero-α-D-manno-heptose-7-phosphate kinase
Reaction: D-glycero-α-D-manno-heptose 7-phosphate + ATP = D-glycero-α-D-manno-heptose 1,7-bisphosphate + ADP
Other name(s): D-α-D-heptose-7-phosphate kinase; hdda (gene name); gmhB (gene name)
Systematic name: ATP:D-glycero-α-D-manno-heptose 7-phosphate 1-phosphotransferase
Comments: The enzyme is involved in biosynthesis of GDP-D-glycero-α-D-manno-heptose, which is required for assembly of S-layer glycoprotein in Gram-positive bacteria. The enzyme is specific for the α-anomer.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Kneidinger, B., Graninger, M., Puchberger, M., Kosma, P. and Messner, P. Biosynthesis of nucleotide-activated D-glycero-D-manno-heptose. J. Biol. Chem. 276 (2001) 20935-20944. [PMID: 11279237]
2. Valvano, M.A., Messner, P. and Kosma, P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 148 (2002) 1979-1989. [PMID: 12101286]
Accepted name: pantoate kinase
Reaction: ATP + (R)-pantoate = ADP + (R)-4-phosphopantoate
Other name(s): PoK; TK2141 protein
Systematic name: ATP:(R)-pantoate 4-phosphotransferase
Comments: The conversion of (R)-pantoate to (R)-4'-phosphopantothenate is part of the pathway leading to biosynthesis of 4'-phosphopantetheine, an essential cofactor of coenzyme A and acyl-carrier protein. In bacteria and eukaryotes this conversion is performed by condensation with β-alanine, followed by phosphorylation (EC 6.3.2.1 and EC 2.7.1.33, respectively). In archaea the order of these two steps is reversed, and phosphorylation precedes condensation with β-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Yokooji, Y., Tomita, H., Atomi, H. and Imanaka, T. Pantoate kinase and phosphopantothenate synthetase, two novel enzymes necessary for CoA biosynthesis in the Archaea. J. Biol. Chem. 284 (2009) 28137-28145. [PMID: 19666462]
Accepted name: anhydro-N-acetylmuramic acid kinase
Reaction: ATP + 1,6-anhydro-N-acetyl-β-muramate + H2O = ADP + N-acetylmuramate 6-phosphate
Other name(s): anhMurNAc kinase; AnmK
Systematic name: ATP:1,6-anhydro-N-acetyl-β-muramate 6-phosphotransferase
Comments: This enzyme, along with EC 4.2.1.126, N-acetylmuramic acid 6-phosphate etherase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling. The product N-acetylmuramate 6-phosphate is produced as a 7:1 mixture of the α- and β-anomers.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M. and Park, J.T. Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J. Bacteriol. 187 (2005) 3643-3649. [PMID: 15901686]
2. Uehara, T., Suefuji, K., Jaeger, T., Mayer, C. and Park, J.T. MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall. J. Bacteriol. 188 (2006) 1660-1662. [PMID: 16452451]
3. Bacik, J.P., Whitworth, G.E., Stubbs, K.A., Yadav, A.K., Martin, D.R., Bailey-Elkin, B.A., Vocadlo, D.J. and Mark, B.L. Molecular basis of 1,6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase. J. Biol. Chem. 286 (2011) 12283-12291. [PMID: 21288904]
Accepted name: protein-fructosamine 3-kinase
Reaction: ATP + [protein]-N6-D-fructosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
Other name(s): FN3K; fructosamine 3-kinase
Systematic name: ATP:[protein]-N6-D-fructosyl-L-lysine 3-phosphotransferase
Comments: Nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as [protein]-N6-D-fructosyl-L-lysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins. The phosphorylation destablilizes the [protein]-N6-D-fructosyl-L-lysine adduct and leads to its spontaneous decomposition. cf. EC 2.7.1.172, protein-ribulosamine 3-kinase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Szwergold, B.S., Howell, S. and Beisswenger, P.J. Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. Diabetes 50 (2001) 2139-2147. [PMID: 11522682]
2. Delpierre, G., Rider, M.H., Collard, F., Stroobant, V., Vanstapel, F., Santos, H. and Van Schaftingen, E. Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. Diabetes 49 (2000) 1627-1634. [PMID: 11016445]
Accepted name: protein-ribulosamine 3-kinase
Reaction: ATP + [protein]-N6-D-ribulosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-ribulosyl)-L-lysine
Other name(s): Fn3KRP; FN3K-related protein; FN3K-RP; ketosamine 3-kinase 2; fructosamine-3-kinase-related protein; ribulosamine/erythrulosamine 3-kinase; ribulosamine 3-kinase
Systematic name: ATP:[protein]-N6-D-ribulosyl-L-lysine 3-phosphotransferase
Comments: This enzyme plays a role in freeing proteins from ribulosamines or psicosamines, which might arise from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by EC 2.7.1.171 (protein-fructosamine 3-kinase), which has, in addition, the unique capacity to phosphorylate fructosamines [1]. The plant enzyme also phosphorylates [protein]-N6-D-erythrulosyl-L-lysine [2]. No activity with [protein]-N6-D-fructosyl-L-lysine [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Collard, F., Delpierre, G., Stroobant, V., Matthijs, G. and Van Schaftingen, E. A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines. Diabetes 52 (2003) 2888-2895. [PMID: 14633848]
2. Fortpied, J., Gemayel, R., Stroobant, V. and van Schaftingen, E. Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme. Biochem. J. 388 (2005) 795-802. [PMID: 15705060]
3. Payne, L.S., Brown, P.M., Middleditch, M., Baker, E., Cooper, G.J. and Loomes, K.M. Mapping of the ATP-binding domain of human fructosamine 3-kinase-related protein by affinity labelling with 5'-[p-(fluorosulfonyl)benzoyl]adenosine. Biochem. J. 416 (2008) 281-288. [PMID: 18637789]
Accepted name: nicotinate riboside kinase
Reaction: ATP + β-D-ribosylnicotinate = ADP + nicotinate β-D-ribonucleotide
Other name(s): ribosylnicotinic acid kinase; nicotinic acid riboside kinase; NRK1 (ambiguous)
Systematic name: ATP:β-D-ribosylnicotinate 5-phosphotransferase
Comments: The enzyme from yeast and human also has the activity of EC 2.7.1.22 (ribosylnicotinamide kinase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Tempel, W., Rabeh, W.M., Bogan, K.L., Belenky, P., Wojcik, M., Seidle, H.F., Nedyalkova, L., Yang, T., Sauve, A.A., Park, H.W. and Brenner, C. Nicotinamide riboside kinase structures reveal new pathways to NAD+. PLoS Biol. 5 (2007) e263. [PMID: 17914902]
Accepted name: diacylglycerol kinase (CTP)
Reaction: CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate
Glossary: 1,2-diacyl-sn-glycerol 3-phosphate = phosphatidate
Other name(s): DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous); DGK1 (gene name); diacylglycerol kinase (CTP dependent)
Systematic name: CTP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Comments: Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Han, G.S., O'Hara, L., Carman, G.M. and Siniossoglou, S. An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth. J. Biol. Chem. 283 (2008) 20433-20442. [PMID: 18458075]
2. Han, G.S., O'Hara, L., Siniossoglou, S. and Carman, G.M. Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase. J. Biol. Chem. 283 (2008) 20443-20453. [PMID: 18458076]
3. Fakas, S., Konstantinou, C. and Carman, G.M. DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae. J. Biol. Chem. 286 (2011) 1464-1474. [PMID: 21071438]
Accepted name: maltokinase
Reaction: ATP + maltose = ADP + α-maltose-1-phosphate
Systematic name: ATP:maltose 1-phosphotransferase
Comments: Requires Mg2+ for activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Mendes, V., Maranha, A., Lamosa, P., da Costa, M.S. and Empadinhas, N. Biochemical characterization of the maltokinase from Mycobacterium bovis BCG. BMC Biochem. 11 (2010) 21. [PMID: 20507595]
Accepted name: UDP-N-acetylglucosamine kinase
Reaction: ATP + UDP-N-acetyl-α-D-glucosamine = ADP + UDP-N-acetyl-α-D-glucosamine 3'-phosphate
Other name(s): UNAG kinase; ζ toxin; toxin PezT
Systematic name: ATP:UDP-N-acetyl-α-D-glucosamine 3'-phosphotransferase
Comments: Toxic component of a toxin-antitoxin (TA) module. The phosphorylation of UDP-N-acetyl-D-glucosamine results in the inhibition of EC 2.5.1.7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, the first committed step in cell wall synthesis, which is then blocked. The activity of this enzyme is inhibited when the enzyme binds to the cognate ε antitoxin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Mutschler, H., Gebhardt, M., Shoeman, R.L. and Meinhart, A. A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis. PLoS Biol 9 (2011) e1001033. [PMID: 21445328]
2. Khoo, S.K., Loll, B., Chan, W.T., Shoeman, R.L., Ngoo, L., Yeo, C.C. and Meinhart, A. Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae. J. Biol. Chem. 282 (2007) 19606-19618. [PMID: 17488720]
Accepted name: L-threonine kinase
Reaction: ATP + L-threonine = ADP + O-phospho-L-threonine
For diagram of reaction click here.
Other name(s): PduX
Systematic name: ATP:L-threonine O3-phosphotransferase
Comments: The enzyme is involved in the de novo synthesis of adenosylcobalamin. It is specific for ATP and free L-threonine. In the bacterium Salmonella enterica the activity with CTP, GTP, or UTP is 6, 11, and 3% of the activity with ATP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Fan, C. and Bobik, T.A. The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B12 synthesis. J. Biol. Chem. 283 (2008) 11322-11329. [PMID: 18308727]
2. Fan, C., Fromm, H.J. and Bobik, T.A. Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica. J. Biol. Chem. 284 (2009) 20240-20248. [PMID: 19509296]
Accepted name: 2-dehydro-3-deoxyglucono/galactono-kinase
Reaction: (1) ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate
(2) ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate
For diagram of reaction click here.
Other name(s): KDG kinase (ambiguous); KDGK (ambiguous); 2-keto-3-deoxy-D-gluconate kinase (ambiguous)
Systematic name: ATP:2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-D-galactonate 6-phosphotransferase
Comments: The enzyme from the archaeon Sulfolobus solfataricus is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It phosphorylates 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with similar catalytic efficiency. cf. EC 2.7.1.45, 2-dehydro-3-deoxygluconokinase and EC 2.7.1.58, 2-dehydro-3-deoxygalactonokinase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Lamble, H.J., Theodossis, A., Milburn, C.C., Taylor, G.L., Bull, S.D., Hough, D.W. and Danson, M.J. Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus. FEBS Lett 579 (2005) 6865-6869. [PMID: 16330030]
2. Potter, J.A., Kerou, M., Lamble, H.J., Bull, S.D., Hough, D.W., Danson, M.J. and Taylor, G.L. The structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase. Acta Crystallogr. D Biol. Crystallogr. 64 (2008) 1283-1287. [PMID: 19018105]
3. Kim, S. and Lee, S.B. Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate kinase in the modified Entner-Doudoroff pathway. Biosci. Biotechnol. Biochem. 70 (2006) 1308-1316. [PMID: 16794308]
Accepted name: kanosamine kinase
Reaction: ATP + kanosamine = ADP + kanosamine 6-phosphate
Glossary: kanosamine = 3-amino-3-deoxy-D-glucose
Other name(s): rifN (gene name)
Systematic name: ATP:kanosamine 6-phosphotransferase
Comments: The enzyme from the bacterium Amycolatopsis mediterranei is specific for kanosamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Arakawa, K., Muller, R., Mahmud, T., Yu, T.W. and Floss, H.G. Characterization of the early stage aminoshikimate pathway in the formation of 3-amino-5-hydroxybenzoic acid: the RifN protein specifically converts kanosamine into kanosamine 6-phosphate. J. Am. Chem. Soc. 124 (2002) 10644-10645. [PMID: 12207505]
Accepted name: FAD:protein FMN transferase
Reaction: FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP
Other name(s): flavin transferase; apbE (gene name)
Systematic name: FAD:protein riboflavin-5'-phosphate transferase
Comments: The enzyme catalyses the transfer of the FMN portion of FAD and its covalent binding to the hydroxyl group of an L-threonine residue in a target flavin-binding protein such as the B and C subunits of EC 7.2.1.1, NADH:ubiquinone reductase (Na+-transporting). Requires Mg2+.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Bertsova, Y.V., Fadeeva, M.S., Kostyrko, V.A., Serebryakova, M.V., Baykov, A.A. and Bogachev, A.V. Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins. J. Biol. Chem 288 (2013) 14276-14286. [PMID: 23558683]
Accepted name: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
Reaction: ATP + α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol = ADP + 3-O-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol
Other name(s): WbdD; ATP:α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Man-(1→3)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phosphotransferase
Systematic name: ATP:α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phosphotransferase
Comments: The enzyme is involved in the biosynthesis of the polymannose O-polysaccharide in the outer leaflet of the membrane of Escherichia coli serotype O9a. O-Polysaccharide structures vary extensively because of differences in the number and type of sugars in the repeat unit. The dual kinase/methylase WbdD also catalyses the methylation of 3-phospho-α-D-Man-(1→2)-α-D-Man-(1→2)-[α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)]n-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-Man-(1→3)-α-D-GlcNAc-diphospho-ditrans,octacis-undecaprenol (cf. EC 2.1.1.294, 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Clarke, B.R., Cuthbertson, L. and Whitfield, C. Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter. J. Biol. Chem. 279 (2004) 35709-35718. [PMID: 15184370]
2. Clarke, B.R., Greenfield, L.K., Bouwman, C. and Whitfield, C. Coordination of polymerization, chain termination, and export in assembly of the Escherichia coli lipopolysaccharide O9a antigen in an ATP-binding cassette transporter-dependent pathway. J. Biol. Chem. 284 (2009) 30662-30672. [PMID: 19734145]
3. Clarke, B.R., Richards, M.R., Greenfield, L.K., Hou, D., Lowary, T.L. and Whitfield, C. In vitro reconstruction of the chain termination reaction in biosynthesis of the Escherichia coli O9a O-polysaccharide: the chain-length regulator, WbdD, catalyzes the addition of methyl phosphate to the non-reducing terminus of the growing glycan. J. Biol. Chem. 286 (2011) 41391-41401. [PMID: 21990359]
4. Liston, S.D., Clarke, B.R., Greenfield, L.K., Richards, M.R., Lowary, T.L. and Whitfield, C. Domain interactions control complex formation and polymerase specificity in the biosynthesis of the Escherichia coli O9a antigen. J. Biol. Chem. 290 (2015) 1075-1085. [PMID: 25422321]
Accepted name: phytol kinase
Reaction: CTP + phytol = CDP + phytyl phosphate
Other name(s): VTE5 (gene name)
Systematic name: CTP:phytol O-phosphotransferase
Comments: The enzyme is found in plants and photosynthetic algae [2] and is involved in phytol salvage [1]. It can use UTP as an alternative phosphate donor with lower activity [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ischebeck, T., Zbierzak, A.M., Kanwischer, M. and Dormann, P. A salvage pathway for phytol metabolism in Arabidopsis. J. Biol. Chem. 281 (2006) 2470-2477. [PMID: 16306049]
2. Valentin, H.E., Lincoln, K., Moshiri, F., Jensen, P.K., Qi, Q., Venkatesh, T.V., Karunanandaa, B., Baszis, S.R., Norris, S.R., Savidge, B., Gruys, K.J. and Last, R.L. The Arabidopsis vitamin E pathway gene5-1 mutant reveals a critical role for phytol kinase in seed tocopherol biosynthesis. Plant Cell 18 (2006) 212-224. [PMID: 16361393]
Accepted name: glycoprotein-mannosyl O6-kinase
Reaction: ATP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl/L-seryl-[protein] = ADP + 3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-6-O-phosphono-α-D-mannosyl]-L-threonyl/L-seryl-[protein]
For diagram of reaction click here.
Other name(s): SGK196; protein O-mannose kinase
Systematic name: ATP:3-O-[N-acetyl-β-D-galactosaminyl-(1→3)-N-acetyl-β-D-glucosaminyl-(1→4)-α-D-mannosyl]-L-threonyl/L-seryl-[protein] 6-phosphotransferase
Comments: In humans this phosphorylated trisaccharide is attached to an L-threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains, and is important for its activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Yoshida-Moriguchi, T., Willer, T., Anderson, M.E., Venzke, D., Whyte, T., Muntoni, F., Lee, H., Nelson, S.F., Yu, L. and Campbell, K.P. SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function. Science 341 (2013) 896-899. [PMID: 23929950]
Accepted name: sulfofructose kinase
Reaction: ATP + 6-deoxy-6-sulfo-D-fructose = ADP + 6-deoxy-6-sulfo-D-fructose 1-phosphate
For diagram of reaction click here.
Other name(s): yihV (gene name)
Systematic name: ATP:6-deoxy-6-sulfo-D-fructose 1-phosphotransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Denger, K., Weiss, M., Felux, A.K., Schneider, A., Mayer, C., Spiteller, D., Huhn, T., Cook, A.M. and Schleheck, D. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. Nature 507 (2014) 114-117. [PMID: 24463506]
Accepted name: mevalonate 3-kinase
Reaction: ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
For diagram of reaction click here.
Other name(s): ATP:(R)-MVA 3-phosphotransferase
Systematic name: ATP:(R)-mevalonate 3-phosphotransferase
Comments: Mevalonate 3-kinase and mevalonate-3-phosphate-5-kinase (EC 2.7.1.186) act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum. Mevalonate 3-kinase is different from mevalonate kinase, EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Vinokur, J.M., Korman, T.P., Cao, Z. and Bowie, J.U. Evidence of a novel mevalonate pathway in archaea. Biochemistry 53 (2014) 4161-4168. [PMID: 24914732]
2. Azami, Y., Hattori, A., Nishimura, H., Kawaide, H., Yoshimura, T. and Hemmi, H. (R)-Mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum. J. Biol. Chem. 289 (2014) 15957-15967. [PMID: 24755225]
Accepted name: mevalonate-3-phosphate 5-kinase
Reaction: ATP + (R)-3-phosphomevalonate = ADP + 3,5-bisphosphomevalonate
For diagram of reaction click here.
Systematic name: ATP:(R)-3-phosphomevalonate 5-phosphotransferase
Comments: Mevalonate 3-kinase (EC 2.7.1.185) and mevalonate-3-phosphate-5-kinase act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Vinokur, J.M., Korman, T.P., Cao, Z. and Bowie, J.U. Evidence of a novel mevalonate pathway in archaea. Biochemistry 53 (2014) 4161-4168. [PMID: 24914732]
Accepted name: acarbose 7IV-phosphotransferase
Reaction: ATP + acarbose = ADP + acarbose 7IV-phosphate
Glossary: acarbose = 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)-2-cyclohexen-1-yl]amino}-α-D-glucopyranosyl-(1→4)-α-D-glucopyranosyl-(1→4)-β-D-glucopyranose
Other name(s): acarbose 7-kinase; AcbK
Systematic name: ATP:acarbose 7IV-phosphotransferase
Comments: The enzyme, characterized from the bacterium Actinoplanes sp. SE50/110, is specific for acarbose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Drepper, A. and Pape, H. Acarbose 7-phosphotransferase from Actinoplanes sp.: purification, properties, and possible physiological function. J. Antibiot. (Tokyo) 49 (1996) 664-668. [PMID: 8784428]
2. Goeke, K., Drepper, A. and Pape, H. Formation of acarbose phosphate by a cell-free extract from the acarbose producer Actinoplanes sp. J. Antibiot. (Tokyo) 49 (1996) 661-663. [PMID: 8784426]
3. Zhang, C.S., Stratmann, A., Block, O., Bruckner, R., Podeschwa, M., Altenbach, H.J., Wehmeier, U.F. and Piepersberg, W. Biosynthesis of the C7-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor leads to proposal of a new biosynthetic pathway. J. Biol. Chem. 277 (2002) 22853-22862. [PMID: 11937512]
Accepted name: 2-epi-5-epi-valiolone 7-kinase
Reaction: ATP + 2-epi-5-epi-valiolone = ADP + 2-epi-5-epi-valiolone 7-phosphate
For diagram of reaction click here.
Glossary: 2-epi-5-epi-valiolone = (2S,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one
Other name(s): AcbM
Systematic name: ATP:2-epi-5-epi-valiolone 7-phosphotransferase
Comments: The enzyme, characterized from the bacterium Actinoplanes sp. SE50/110, is involved in the biosynthesis of the oligosaccharide acarbose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, C.S., Stratmann, A., Block, O., Bruckner, R., Podeschwa, M., Altenbach, H.J., Wehmeier, U.F. and Piepersberg, W. Biosynthesis of the C7-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor leads to proposal of a new biosynthetic pathway. J. Biol. Chem. 277 (2002) 22853-22862. [PMID: 11937512]
Accepted name: autoinducer-2 kinase
Reaction: ATP + (S)-4,5-dihydroxypentane-2,3-dione = ADP + (S)-4-hydroxypentane-2,3-dione 5-phosphate
Glossary: (S)-4,5-dihydroxypentane-2,3-dione = autoinducer 2 = AI-2
Other name(s): lsrK (gene name)
Systematic name: ATP:(S)-4,5-dihydroxypentane-2,3-dione 5-phosphotransferase
Comments: The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Xavier, K.B., Miller, S.T., Lu, W., Kim, J.H., Rabinowitz, J., Pelczer, I., Semmelhack, M.F. and Bassler, B.L. Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria. ACS Chem. Biol. 2 (2007) 128-136. [PMID: 17274596]
2. Roy, V., Fernandes, R., Tsao, C.Y. and Bentley, W.E. Cross species quorum quenching using a native AI-2 processing enzyme. ACS Chem. Biol. 5 (2010) 223-232. [PMID: 20025244]
3. Zhu, J., Hixon, M.S., Globisch, D., Kaufmann, G.F. and Janda, K.D. Mechanistic insights into the LsrK kinase required for autoinducer-2 quorum sensing activation. J. Am. Chem. Soc. 135 (2013) 7827-7830. [PMID: 23672516]
Accepted name: aminoglycoside 2''-phosphotransferase
Reaction: GTP + gentamicin = GDP + gentamicin 2''-phosphate
Other name(s): aphD (gene name); APH(2''); aminoglycoside (2'') kinase; gentamicin kinase (ambiguous); gentamicin phosphotransferase (ambiguous)
Systematic name: GTP:gentamicin 2''-O-phosphotransferase
Comments: Requires Mg2+. This bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. In most, but not all, cases the phosphorylation confers resistance against the antibiotic. Some forms of the enzyme use ATP as a phosphate donor in appreciable amount. The enzyme is often found as a bifunctional enzyme that also catalyses 6'-aminoglycoside N-acetyltransferase activity. The bifunctional enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Ferretti, J.J., Gilmore, K.S. and Courvalin, P. Nucleotide sequence analysis of the gene specifying the bifunctional 6'-aminoglycoside acetyltransferase 2"-aminoglycoside phosphotransferase enzyme in Streptococcus faecalis and identification and cloning of gene regions specifying the two activities. J. Bacteriol. 167 (1986) 631-638. [PMID: 3015884]
2. Frase, H., Toth, M. and Vakulenko, S.B. Revisiting the nucleotide and aminoglycoside substrate specificity of the bifunctional aminoglycoside acetyltransferase(6')-Ie/aminoglycoside phosphotransferase(2'')-Ia enzyme. J. Biol. Chem. 287 (2012) 43262-43269. [PMID: 23115238]
Accepted name: protein-Nπ-phosphohistidine—D-mannose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + D-mannose[side 1] = [protein]-L-histidine + D-mannose 6-phosphate[side 2]
Other name(s): manXYZ (gene names); mannose PTS permease; EIIMan; Enzyme IIMan
Systematic name: protein-Nπ-phospho-L-histidine:D-mannose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Erni, B. and Zanolari, B. The mannose-permease of the bacterial phosphotransferase system. Gene cloning and purification of the enzyme IIMan/IIIMan complex of Escherichia coli, J. Biol. Chem. 260 (1985) 15495-15503. [PMID: 2999119]
2. Williams, N., Fox, D.K., Shea, C. and Roseman, S. Pel, the protein that permits lambda DNA penetration of Escherichia coli, is encoded by a gene in ptsM and is required for mannose utilization by the phosphotransferase system. Proc. Natl. Acad. Sci. USA 83 (1986) 8934-8938. [PMID: 2947241]
3. Erni, B., Zanolari, B. and Kocher, H.P. The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA. J. Biol. Chem. 262 (1987) 5238-5247. [PMID: 2951378]
4. Stolz, B., Huber, M., Markovic-Housley, Z. and Erni, B. The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit. J. Biol. Chem. 268 (1993) 27094-27099. [PMID: 8262947]
5. Rhiel, E., Flukiger, K., Wehrli, C. and Erni, B. The mannose transporter of Escherichia coli K12: oligomeric structure, and function of two conserved cysteines. Biol Chem Hoppe Seyler 375 (1994) 551-559. [PMID: 7811395]
6. Huber, F. and Erni, B. Membrane topology of the mannose transporter of Escherichia coli K12. Eur. J. Biochem. 239 (1996) 810-817. [PMID: 8774730]
Accepted name: protein-Nπ-phosphohistidine—N-acetyl-D-muramate phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + N-acetyl-D-muramate[side 1] = [protein]-L-histidine + N-acetyl-D-muramate 6-phosphate[side 2]
Other name(s): murP (gene name); N-acetylmuramic acid PTS permease; EIINAcMur; Enzyme IINAcMur
Systematic name: protein-Nπ-phospho-L-histidine:N-acetyl-D-muramate Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Dahl, U., Jaeger, T., Nguyen, B.T., Sattler, J.M. and Mayer, C. Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid. J. Bacteriol. 186 (2004) 2385-2392. [PMID: 15060041]
Accepted name: protein-Nπ-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + N-acetyl-D-glucosamine[side 1] = [protein]-L-histidine + N-acetyl-D-glucosamine 6-phosphate[side 2]
Other name(s): nagE (gene name); N-acetyl-D-glucosamine PTS permease; EIINag; Enzyme IINag; EIICBANag
Systematic name: protein-Nπ-phospho-L-histidine:N-acetyl-D-glucosamine Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. White, R.J. The role of the phosphoenolpyruvate phosphotransferase system in the transport of N-acetyl-D-glucosamine by Escherichia coli, Biochem. J. 118 (1970) 89-92. [PMID: 4919472]
2. Rogers, M.J., Ohgi, T., Plumbridge, J. and Soll, D. Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase. Gene 62 (1988) 197-207. [PMID: 3284790]
3. Peri, K.G. and Waygood, E.B. Sequence of cloned enzyme IIN-acetylglucosamine of the phosphoenolpyruvate:N-acetylglucosamine phosphotransferase system of Escherichia coli. Biochemistry 27 (1988) 6054-6061. [PMID: 3056518]
4. Plumbridge, J. An alternative route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in Escherichia coli, J. Bacteriol. 191 (2009) 5641-5647. [PMID: 19617367]
Accepted name: protein-Nπ-phosphohistidine—L-ascorbate phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + L-ascorbate[side 1] = [protein]-L-histidine + L-ascorbate 6-phosphate[side 2]
Other name(s): ulaABC (gene names); L-ascorbate PTS permease; EIISga; Enzyme IISga; Enzyme IIUla
Systematic name: protein-Nπ-phospho-L-histidine:L-ascorbate Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, Z., Aboulwafa, M., Smith, M.H. and Saier, M.H., Jr. The ascorbate transporter of Escherichia coli, J. Bacteriol. 185 (2003) 2243-2250. [PMID: 12644495]
2. Hvorup, R., Chang, A.B. and Saier, M.H., Jr. Bioinformatic analyses of the bacterial L-ascorbate phosphotransferase system permease family. J. Mol. Microbiol. Biotechnol. 6 (2003) 191-205. [PMID: 15153772]
3. Luo, P., Yu, X., Wang, W., Fan, S., Li, X. and Wang, J. Crystal structure of a phosphorylation-coupled vitamin C transporter. Nat. Struct. Mol. Biol. 22 (2015) 238-241. [PMID: 25686089]
Accepted name: protein-Nπ-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + 2-O-α-mannosyl-D-glycerate [side 1] = [protein]-L-histidine + 2-O-(6-phospho-α-D-mannosyl)-D-glycerate [side 2]
Other name(s): mngA (gene names); 2-O-α-mannosyl-D-glycerate PTS permease; EIIMngA; Enzyme IIMngA; Enzyme IIHrsA; EIImannosylglycerate; Frx
Systematic name: protein-Nπ-phospho-L-histidine:2-O-α-mannosyl-D-glycerate Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sampaio, M.M., Chevance, F., Dippel, R., Eppler, T., Schlegel, A., Boos, W., Lu, Y.J. and Rock, C.O. Phosphotransferase-mediated transport of the osmolyte 2-O-α-mannosyl-D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA) gene and is regulated by the mngR (farR) gene product acting as repressor. J. Biol. Chem. 279 (2004) 5537-5548. [PMID: 14645248]
Accepted name: protein-Nπ-phosphohistidine—N,N'-diacetylchitobiose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + N,N'-diacetylchitobiose[side 1] = [protein]-L-histidine + N,N'-diacetylchitobiose 6'-phosphate[side 2]
Other name(s): chbABC (gene names); N,N'-diacetylchitobiose PTS permease; chitobiose PTS permease; EIIcel; EIIchb; Enzyme IIcel; Enzyme IIchb
Systematic name: protein-Nπ-phospho-L-histidine:N,N'-diacetylchitobiose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Keyhani, N.O., Wang, L.X., Lee, Y.C. and Roseman, S. The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J. Biol. Chem. 275 (2000) 33084-33090. [PMID: 10913117]
2. Reizer, J., Reizer, A. and Saier, M.H., Jr. The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus, Res. Microbiol. 141 (1990) 1061-1067. [PMID: 2092358]
3. Keyhani, N.O., Boudker, O. and Roseman, S. Isolation and characterization of IIAChb, a soluble protein of the enzyme II complex required for the transport/phosphorylation of N, N'-diacetylchitobiose in Escherichia coli, J. Biol. Chem. 275 (2000) 33091-33101. [PMID: 10913118]
4. Keyhani, N.O., Bacia, K. and Roseman, S. The transport/phosphorylation of N,N'-diacetylchitobiose in Escherichia coli. Characterization of phospho-IIB(Chb) and of a potential transition state analogue in the phosphotransfer reaction between the proteins IIA(Chb) AND IIB(Chb). J. Biol. Chem. 275 (2000) 33102-33109. [PMID: 10913119]
Accepted name: protein-Nπ-phosphohistidine—D-mannitol phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + D-mannitol[side 1] = [protein]-L-histidine + D-mannitol 1-phosphate[side 2]
Other name(s): mtlA (gene name); D-mannitol PTS permease; EIIMtl
Systematic name: protein-Nπ-phospho-L-histidine:D-mannitol Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Jacobson, G.R., Lee, C.A. and Saier, M.H., Jr. Purification of the mannitol-specific enzyme II of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. J. Biol. Chem. 254 (1979) 249-252. [PMID: 368051]
2. Jacobson, G.R., Tanney, L.E., Kelly, D.M., Palman, K.B. and Corn, S.B. Substrate and phospholipid specificity of the purified mannitol permease of Escherichia coli, J. Cell. Biochem. 23 (1983) 231-240. [PMID: 6427236]
3. Lee, C.A. and Saier, M.H., Jr. Mannitol-specific enzyme II of the bacterial phosphotransferase system. III. The nucleotide sequence of the permease gene. J. Biol. Chem. 258 (1983) 10761-10767. [PMID: 6309813]
4. Elferink, M.G., Driessen, A.J. and Robillard, G.T. Functional reconstitution of the purified phosphoenolpyruvate-dependent mannitol-specific transport system of Escherichia coli in phospholipid vesicles: coupling between transport and phosphorylation. J. Bacteriol. 172 (1990) 7119-7125. [PMID: 2123863]
5. van Weeghel, R.P., Meyer, G., Pas, H.H., Keck, W. and Robillard, G.T. Cytoplasmic phosphorylating domain of the mannitol-specific transport protein of the phosphoenolpyruvate-dependent phosphotransferase system in Escherichia coli: overexpression, purification, and functional complementation with the mannitol binding domain. Biochemistry 30 (1991) 9478-9485. [PMID: 1909895]
6. Boer, H., ten Hoeve-Duurkens, R.H. and Robillard, G.T. Relation between the oligomerization state and the transport and phosphorylation function of the Escherichia coli mannitol transport protein: interaction between mannitol-specific enzyme II monomers studied by complementation of inactive site-directed mutants. Biochemistry 35 (1996) 12901-12908. [PMID: 8841134]
Accepted name: protein-Nπ-phosphohistidine—D-sorbitol phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + D-sorbitol[side 1] = [protein]-L-histidine + D-sorbitol 6-phosphate[side 2]
Other name(s): srlABE (gene names); D-sorbitol PTS permease; sorbitol PTS permease; glucitol PTS permease; EIIGut; Enzyme IIGut
Systematic name: protein-Nπ-phospho-L-histidine:D-sorbitol Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lengeler, J. Nature and properties of hexitol transport systems in Escherichia coli, J. Bacteriol. 124 (1975) 39-47. [PMID: 1100608]
2. Reizer, J., Mitchell, W.J., Minton, N., Brehm, J., Reizer, A. and Saier, M.H., Jr. Proposed topology of the glucitol permeases of Escherichia coli and Clostridium acetobutylicum, Curr. Microbiol. 33 (1996) 331-333. [PMID: 8875915]
Accepted name: protein-Nπ-phosphohistidine—D-glucose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + D-glucose[side 1] = [protein]-L-histidine + D-glucose 6-phosphate[side 2]
Other name(s): ptsG (gene name); D-glucose PTS permease; EIIGlc; Enzyme IIGlc
Systematic name: protein-Nπ-phospho-L-histidine:D-glucose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Stock, J.B., Waygood, E.B., Meadow, N.D., Postma, P.W. and Roseman, S. Sugar transport by the bacterial phosphotransferase system. The glucose receptors of the Salmonella typhimurium phosphotransferase system. J. Biol. Chem. 257 (1982) 14543-14552. [PMID: 6292227]
2. Erni, B. and Zanolari, B. Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc. J. Biol. Chem. 261 (1986) 16398-16403. [PMID: 3023349]
Accepted name: protein-Nπ-phosphohistidine—galactitol phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + galactitol[side 1] = [protein]-L-histidine + galactitol 1-phosphate[side 2]
Other name(s): gatABC (gene names); galactitol PTS permease; EIIGat; Enzyme IIGat
Systematic name: protein-Nπ-phospho-L-histidine:galactitol Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lengeler, J. Nature and properties of hexitol transport systems in Escherichia coli, J. Bacteriol. 124 (1975) 39-47. [PMID: 1100608]
2. Nobelmann, B. and Lengeler, J.W. Sequence of the gat operon for galactitol utilization from a wild-type strain EC3132 of Escherichia coli, Biochim. Biophys. Acta 1262 (1995) 69-72. [PMID: 7772602]
3. Nobelmann, B. and Lengeler, J.W. Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism. J. Bacteriol. 178 (1996) 6790-6795. [PMID: 8955298]
Accepted name: protein-Nπ-phosphohistidine—trehalose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + α,α-trehalose[side 1] = [protein]-L-histidine + α,α-trehalose 6-phosphate[side 2]
Other name(s): treB (gene name); trehalose PTS permease; EIITre; Enzyme IITre
Systematic name: protein-Nπ-phospho-L-histidine:α,α-trehalose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Boos, W., Ehmann, U., Forkl, H., Klein, W., Rimmele, M. and Postma, P. Trehalose transport and metabolism in Escherichia coli, J. Bacteriol. 172 (1990) 3450-3461. [PMID: 2160944]
2. Klein, W., Horlacher, R. and Boos, W. Molecular analysis of treB encoding the Escherichia coli enzyme II specific for trehalose. J. Bacteriol. 177 (1995) 4043-4052. [PMID: 7608078]
Accepted name: protein-Nπ-phosphohistidine—D-fructose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + D-fructose[side 1] = [protein]-L-histidine + D-fructose 1-phosphate[side 2]
Other name(s): fruAB (gene names); fructose PTS permease; EIIFru; Enzyme IIFru
Systematic name: protein-Nπ-phospho-L-histidine:D-fructose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is usually a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). The enzyme from the bacterium Escherichia coli is an exception, since it is phosphorylated directly by EC 2.7.3.9. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Waygood, E.B. Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components: enzyme IIfructose and fructose-induced HPr-like protein (FPr). Can. J. Biochem. 58 (1980) 1144-1146. [PMID: 7006754]
2. Kornberg, H. The roles of HPr and FPr in the utilization of fructose by Escherichia coli, FEBS Lett. 194 (1986) 12-15. [PMID: 3510127]
3. Geerse, R.H., Izzo, F. and Postma, P.W. The PEP: fructose phosphotransferase system in Salmonella typhimurium: FPr combines enzyme IIIFru and pseudo-HPr activities. Mol. Gen. Genet. 216 (1989) 517-525. [PMID: 2546043]
4. Kornberg, H.L. and Lambourne, L.T. Role of the phosphoenolpyruvate-dependent fructose phosphotransferase system in the utilization of mannose by Escherichia coli, Proc Biol Sci 250 (1992) 51-55. [PMID: 1361062]
Accepted name: protein-Nπ-phosphohistidine—D-glucosaminate phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + 2-amino-2-deoxy-D-gluconate[side 1] = [protein]-L-histidine + 2-amino-2-deoxy-D-gluconate 6-phosphate[side 2]
Other name(s): dgaABCD (gene names); 2-amino-2-deoxy-D-gluconate PTS permease
Systematic name: protein-Nπ-phospho-L-histidine:2-amino-2-deoxy-D-gluconate Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Miller, K.A., Phillips, R.S., Mrazek, J. and Hoover, T.R. Salmonella utilizes D-glucosaminate via a mannose family phosphotransferase system permease and associated enzymes. J. Bacteriol. 195 (2013) 4057-4066. [PMID: 23836865]
Accepted name: protein-Nπ-phosphohistidine—D-galactose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + D-galactose[side 1] = [protein]-L-histidine + D-galactose 6-phosphate[side 2]
Other name(s): D-galactose PTS permease; EIIGal; Enzyme IIGal
Systematic name: protein-Nπ-phospho-L-histidine:D-galactose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zeng, L., Martino, N.C. and Burne, R.A. Two gene clusters coordinate galactose and lactose metabolism in Streptococcus gordonii, Appl. Environ. Microbiol. 78 (2012) 5597-5605. [PMID: 22660715]
2. Zeng, L., Xue, P., Stanhope, M.J. and Burne, R.A. A galactose-specific sugar: phosphotransferase permease is prevalent in the non-core genome of Streptococcus mutans, Mol Oral Microbiol 28 (2013) 292-301. [PMID: 23421335]
Accepted name: protein-Nπ-phosphohistidine—D-cellobiose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + D-cellobiose[side 1] = [protein]-L-histidine + D-cellobiose 6'-phosphate[side 2]
Other name(s): celB (gene name); D-cellobiose PTS permease; EIICel; Enzyme IICel
Systematic name: protein-Nπ-phospho-L-histidine:D-cellobiose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Lai, X. and Ingram, L.O. Cloning and sequencing of a cellobiose phosphotransferase system operon from Bacillus stearothermophilus XL-65-6 and functional expression in Escherichia coli, J. Bacteriol. 175 (1993) 6441-6450. [PMID: 8407820]
2. Lai, X., Davis, F.C., Hespell, R.B. and Ingram, L.O. Cloning of cellobiose phosphoenolpyruvate-dependent phosphotransferase genes: functional expression in recombinant Escherichia coli and identification of a putative binding region for disaccharides. Appl. Environ. Microbiol. 63 (1997) 355-363. [PMID: 9023916]
3. Stoll, R. and Goebel, W. The major PEP-phosphotransferase systems (PTSs) for glucose, mannose and cellobiose of Listeria monocytogenes, and their significance for extra- and intracellular growth. Microbiology 156 (2010) 1069-1083. [PMID: 20056707]
4. Wu, M.C., Chen, Y.C., Lin, T.L., Hsieh, P.F. and Wang, J.T. Cellobiose-specific phosphotransferase system of Klebsiella pneumoniae and its importance in biofilm formation and virulence. Infect. Immun. 80 (2012) 2464-2472. [PMID: 22566508]
Accepted name: protein-Nπ-phosphohistidine—L-sorbose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + L-sorbose[side 1] = [protein]-L-histidine + L-sorbose 1-phosphate[side 2]
Other name(s): sorABFM (gene names); L-sorbose PTS permease; EIISor; Enzyme IISor
Systematic name: protein-Nπ-phospho-L-histidine:L-sorbose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wehmeier, U.F., Wohrl, B.M. and Lengeler, J.W. Molecular analysis of the phosphoenolpyruvate-dependent L-sorbose: phosphotransferase system from Klebsiella pneumoniae and of its multidomain structure. Mol. Gen. Genet. 246 (1995) 610-618. [PMID: 7700234]
2. Yebra, M.J., Veyrat, A., Santos, M.A. and Perez-Martinez, G. Genetics of L-sorbose transport and metabolism in Lactobacillus casei, J. Bacteriol. 182 (2000) 155-163. [PMID: 10613875]
Accepted name: protein-Nπ-phosphohistidine—lactose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + lactose[side 1] = [protein]-L-histidine + lactose 6'-phosphate[side 2]
Other name(s): lacEF (gene names); lactose PTS permease; EIILac; Enzyme IILac
Systematic name: protein-Nπ-phospho-L-histidine:lactose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Hengstenberg, W. Solubilization of the membrane bound lactose specific component of the staphylococcal PEP dependant phosphotransferase system. FEBS Lett. 8 (1970) 277-280. [PMID: 11947593]
2. Vadeboncoeur, C. and Proulx, M. Lactose transport in Streptococcus mutans: isolation and characterization of factor IIIlac, a specific protein component of the phosphoenolpyruvate-lactose phosphotransferase system. Infect. Immun. 46 (1984) 213-219. [PMID: 6480107]
3. Breidt, F., Jr., Hengstenberg, W., Finkeldei, U. and Stewart, G.C. Identification of the genes for the lactose-specific components of the phosphotransferase system in the lac operon of Staphylococcus aureus, J. Biol. Chem. 262 (1987) 16444-16449. [PMID: 2824493]
4. De Vos, W.M., Boerrigter, I., Van Rooijen, R.J., Reiche, B., Hengstenberg, W. Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis, J. Biol. Chem. 265 (1990) 22554-22560. [PMID: 2125052]
5. Peters, D., Frank, R. and Hengstenberg, W. Lactose-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. Purification of the histidine-tagged transmembrane component IICBLac and its hydrophilic IIB domain by metal-affinity chromatography, and functional characterization. Eur. J. Biochem. 228 (1995) 798-804. [PMID: 7737179]
Accepted name: protein-Nπ-phosphohistidine—maltose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + maltose[side 1] = [protein]-L-histidine + maltose 6'-phosphate[side 2]
Other name(s): malT (gene name); maltose PTS permease; EIIMal; Enzyme IIMal
Systematic name: protein-Nπ-phospho-L-histidine:maltose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Robrish, S.A., Fales, H.M., Gentry-Weeks, C. and Thompson, J. Phosphoenolpyruvate-dependent maltose:phosphotransferase activity in Fusobacterium mortiferum ATCC 25557: specificity, inducibility, and product analysis. J. Bacteriol. 176 (1994) 3250-3256. [PMID: 8195080]
2. Webb, A.J., Homer, K.A. and Hosie, A.H. A phosphoenolpyruvate-dependent phosphotransferase system is the principal maltose transporter in Streptococcus mutans, J. Bacteriol. 189 (2007) 3322-3327. [PMID: 17277067]
Accepted name: L-erythrulose 1-kinase
Reaction: ATP + L-erythrulose = ADP + L-erythrulose 1-phosphate
Other name(s): lerK (gene name); L-erythrulose 1-kinase [incorrect]
Systematic name: ATP:L-erythrulose 1-phosphotransferase
Comments: The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of L-threitol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Huang, H., Carter, M.S., Vetting, M.W., Al-Obaidi, N., Patskovsky, Y., Almo, S.C. and Gerlt, J.A. A general strategy for the discovery of metabolic pathways: D-threitol, L-threitol, and erythritol utilization in Mycobacterium smegmatis. J. Am. Chem. Soc. 137 (2015) 14570-14573. [PMID: 26560079]
2. Huang, H., Carter, M.S., Vetting, M.W., Al-Obaidi, N., Patskovsky, Y., Almo, S.C. and Gerlt, J.A. Correction to "A general strategy for the discovery of metabolic pathways: D-threitol, L-threitol, and erythritol utilization in Mycobacterium smegmatis". J. Am. Chem. Soc. 138 (2016) 4267. [PMID: 26978037]
Accepted name: D-erythrulose 4-kinase
Reaction: ATP + D-erythrulose = ADP + D-erythrulose 4-phosphate
Other name(s): derK (gene name)
Systematic name: ATP:D-erythrulose 4-phosphotransferase
Comments: The enzyme, characterized from the bacterium Mycobacterium smegmatis, participates in the degradation of erythritol and D-threitol.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Huang, H., Carter, M.S., Vetting, M.W., Al-Obaidi, N., Patskovsky, Y., Almo, S.C. and Gerlt, J.A. A general strategy for the discovery of metabolic pathways: D-threitol, L-threitol, and erythritol utilization in Mycobacterium smegmatis. J. Am. Chem. Soc. 137 (2015) 14570-14573. [PMID: 26560079]
Accepted name: protein-Nπ-phosphohistidine—sucrose phosphotransferase
Reaction: [protein]-Nπ-phospho-L-histidine + sucrose[side 1] = [protein]-L-histidine + sucrose 6G-phosphate[side 2]
Other name(s): scrAB (gene names); sucrose PTS permease; EIIScr; Enzyme IIScr
Systematic name: protein-Nπ-phospho-L-histidine:sucrose Nπ-phosphotransferase
Comments: This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate—protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. St Martin, E.J. and Wittenberger, C.L. Characterization of a phosphoenolpyruvate-dependent sucrose phosphotransferase system in Streptococcus mutans. Infect. Immun. 24 (1979) 865-868. [PMID: 468378]
2. Lunsford, R.D. and Macrina, F.L. Molecular cloning and characterization of scrB, the structural gene for the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system sucrose-6-phosphate hydrolase. J. Bacteriol. 166 (1986) 426-434. [PMID: 3009399]
3. Fouet, A., Arnaud, M., Klier, A. and Rapoport, G. Bacillus subtilis sucrose-specific enzyme II of the phosphotransferase system: expression in Escherichia coli and homology to enzymes II from enteric bacteria. Proc. Natl. Acad. Sci. USA 84 (1987) 8773-8777. [PMID: 3122206]
4. Sato, Y., Poy, F., Jacobson, G.R. and Kuramitsu, H.K. Characterization and sequence analysis of the scrA gene encoding enzyme IIScr of the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system. J. Bacteriol. 171 (1989) 263-271. [PMID: 2536656]
5. Titgemeyer, F., Jahreis, K., Ebner, R. and Lengeler, J.W. Molecular analysis of the scrA and scrB genes from Klebsiella pneumoniae and plasmid pUR400, which encode the sucrose transport protein Enzyme II Scr of the phosphotransferase system and a sucrose-6-phosphate invertase. Mol. Gen. Genet. 250 (1996) 197-206. [PMID: 8628219]
6. Jiang, L., Cai, J., Wang, J., Liang, S., Xu, Z. and Yang, S.T. Phosphoenolpyruvate-dependent phosphorylation of sucrose by Clostridium tyrobutyricum ZJU 8235: evidence for the phosphotransferase transport system. Bioresour. Technol. 101 (2010) 304-309. [PMID: 19726178]
Accepted name: α-D-ribose-1-phosphate 5-kinase (ADP)
Reaction: ADP + α-D-ribose-1-phosphate = AMP + α-D-ribose 1,5-bisphosphate
Systematic name: ADP:α-D-ribose-1-phosphate 5-phosphotransferase
Comments: The enzyme, characterized from the archaeon Thermococcus kodakarensis, participates in an archaeal pathway for nucleoside degradation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Aono, R., Sato, T., Imanaka, T. and Atomi, H. A pentose bisphosphate pathway for nucleoside degradation in Archaea. Nat. Chem. Biol. 11 (2015) 355-360. [PMID: 25822915]
Accepted name: cytidine kinase
Reaction: ATP + cytidine = ADP + CMP
Systematic name: ATP:cytidine 5'-phosphotransferase
Comments: The enzyme, characterized from the archaeon Thermococcus kodakarensis, participates in a pathway for nucleoside degradation. The enzyme can also act on deoxycytidine and uridine, but unlike EC 2.7.1.48, uridine kinase, it is most active with cytidine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Aono, R., Sato, T., Imanaka, T. and Atomi, H. A pentose bisphosphate pathway for nucleoside degradation in Archaea. Nat. Chem. Biol. 11 (2015) 355-360. [PMID: 25822915]
Accepted name: C7-cyclitol 7-kinase
Reaction: (1) ATP + valienone = ADP + valienone 7-phosphate
(2) ATP + validone = ADP + validone 7-phosphate
Glossary: valienone = (4R,5S,6R)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-one
validone = (2R,3S,4R,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexan-1-one
Other name(s): valC (gene name); vldC (gene name)
Systematic name: ATP:C7-cyclitol 7-phosphotransferase
Comments: The enzyme, characterized from the bacterium Streptomyces hygroscopicus var. jinggangensis, is involved in the biosynthesis of the antifungal agent validamycin A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Minagawa, K., Zhang, Y., Ito, T., Bai, L., Deng, Z. and Mahmud, T. ValC, a new type of C7-Cyclitol kinase involved in the biosynthesis of the antifungal agent validamycin A. Chembiochem 8 (2007) 632-641. [PMID: 17335096]
Accepted name: erythritol kinase (D-erythritol 1-phosphate-forming)
Reaction: ATP + erythritol = ADP + D-erythritol 1-phosphate
Other name(s): eryA (gene name)
Systematic name: ATP:erythritol 1-phosphotransferase
Comments: The enzyme, characterized from the pathogenic bacterium Brucella abortus, which causes brucellosis in livestock, participates in erythritol catabolism. cf. EC 2.7.1.27, erythritol kinase (D-erythritol 4-phosphate-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sperry, J.F. and Robertson, D.C. Erythritol catabolism by Brucella abortus. J. Bacteriol. 121 (1975) 619-630. [PMID: 163226]
2. Lillo, A.M., Tetzlaff, C.N., Sangari, F.J. and Cane, D.E. Functional expression and characterization of EryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of L-erythritol-4-phosphate. Bioorg. Med. Chem. Lett. 13 (2003) 737-739. [PMID: 12639570]
Accepted name: farnesol kinase
Reaction: CTP + (2E,6E)-farnesol = CDP + (2E,6E)-farnesyl phosphate
For diagram of reaction click here.
Other name(s): FOLK (gene name)
Systematic name: CTP:(2E,6E)-farnesol phosphotransferase
Comments: The enzyme, found in plants and animals, can also use other nucleotide triphosphates as phosphate donor, albeit less efficiently. The plant enzyme can also use geraniol and geranylgeraniol as substrates with lower activity, but not farnesyl phosphate (cf. EC 2.7.4.32, farnesyl phosphate kinase) [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bentinger, M., Grunler, J., Peterson, E., Swiezewska, E. and Dallner, G. Phosphorylation of farnesol in rat liver microsomes: properties of farnesol kinase and farnesyl phosphate kinase. Arch. Biochem. Biophys. 353 (1998) 191-198. [PMID: 9606952]
2. Fitzpatrick, A.H., Bhandari, J. and Crowell, D.N. Farnesol kinase is involved in farnesol metabolism, ABA signaling and flower development in Arabidopsis. Plant J. 66 (2011) 1078-1088. [PMID: 21395888]
Accepted name: 3-dehydrotetronate 4-kinase
Reaction: (1) ATP + 3-dehydro-L-erythronate = ADP + 3-dehydro-4-phospho-L-erythronate
(2) ATP + 3-dehydro-D-erythronate = ADP + 3-dehydro-4-phospho-D-erythronate
For diagram of reaction click here.
Glossary: L-erythronate = (2S,3S)-2,3,4-trihydroxybutanoate
D-erythronate = (2R,3R)-2,3,4-trihydroxybutanoate
Other name(s): otnK (gene name)
Systematic name: ATP:3-dehydrotetronate 4-phosphotransferase
Comments: The enzyme, characterized from bacteria, is involved in D-erythronate and L-threonate catabolism.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]
Accepted name: fructoselysine 6-kinase
Reaction: ATP + N6-(D-fructosyl)-L-lysine = ADP + N6-(6-phospho-D-fructosyl)-L-lysine
Other name(s): frlD (gene name)
Systematic name: ATP:D-fructosyl-L-lysine 6-phosphotransferase
Comments: The enzyme, characterized from the bacterium Escherichia coli, has very little activity with fructose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Wiame, E., Delpierre, G., Collard, F. and Van Schaftingen, E. Identification of a pathway for the utilization of the Amadori product fructoselysine in Escherichia coli. J. Biol. Chem. 277 (2002) 42523-42529. [PMID: 12147680]
2. Wiame, E. and Van Schaftingen, E. Fructoselysine 3-epimerase, an enzyme involved in the metabolism of the unusual Amadori compound psicoselysine in Escherichia coli. Biochem. J. 378 (2004) 1047-1052. [PMID: 14641112]
Accepted name: D-threonate 4-kinase
Reaction: ATP + D-threonate = ADP + 4-phospho-D-threonate
For diagram of reaction click here
Glossary: D-threonate = (2S,3R)-2,3,4-trihydroxybutanoate
Other name(s): dtnK (gene name)
Systematic name: ATP:D-threonate 4-phosphotransferase
Comments: The enzyme, characterized from bacteria, is involved in a pathway for D-threonate catabolism.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]
Accepted name: D-erythronate 4-kinase
Reaction: ATP + D-erythronate = ADP + 4-phospho-D-erythronate
For diagram of reaction click here
Glossary: D-erythronate = (2R,3R)-2,3,4-trihydroxybutanoate
Other name(s): denK (gene name)
Systematic name: ATP:D-erythronate 4-phosphotransferase
Comments: The enzyme, characterized from bacteria, is involved in a pathway for D-erythronate catabolism.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl Acad. Sci. USA 113 (2016) E4161-E4169. [PMID: 27402745]
Accepted name: N-acetylmuramate 1-kinase
Reaction: ATP + N-acetyl-D-muramate = ADP + N-acetyl-α-D-muramate 1-phosphate
Glossary: N-acetyl-D-muramate = 3-O-[(1R)-1-carboxyethyl]-2-acetoxy-2-deoxy-D-glucopyranose
Other name(s): amgK (gene name)
Systematic name: ATP:N-acetyl-D-muramate 1-phosphotransferase
Comments: The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Gisin, J., Schneider, A., Nagele, B., Borisova, M. and Mayer, C. A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis. Nat. Chem. Biol. 9 (2013) 491-493. [PMID: 23831760]
Accepted name: 4-hydroxytryptamine kinase
Reaction: ATP + 4-hydroxytryptamine = ADP + 4-hydoxytryptamine 4-phosphate
For diagram of reaction click here
Glossary: psilocybin = 3-[2-(dimethylamino)ethyl]-1H-indol-4-yl phosphate
Other name(s): PsiK
Systematic name: ATP:4-hydroxytryptamine 4-phosphotransferase
Comments: Also acts on 4-hydroxy-L-tryptophan in vitro. Isolated from the fungus Psilocybe cubensis. Involved in the biosynthesis of the psychoactive compound psilocybin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Fricke, J., Blei, F. and Hoffmeister, D. Enzymatic synthesis of psilocybin. Angew. Chem. Int. Ed. Engl. 56 (2017) 12352-12355.
Accepted name: aminoimidazole riboside kinase
Reaction: ATP + 5-amino-1-(β-D-ribosyl)imidazole = ADP + 5-amino-1-(5-phospho-β-D-ribosyl)imidazole
Other name(s): STM4066 (locus name)
Systematic name: ATP:5-amino-1-(β-D-ribosyl)imidazole 5'-phosphotransferase
Comments: The enzyme, characterized from the bacterium Salmonella enterica, can phosphorylate exogeneously-provided 5-amino-1-(β-D-ribosyl)imidazole to form 5-amino-1-(5-phospho-β-D-ribosyl)imidazole (AIR), an important intermediate in the production of both purine mononucleotides and the hydroxymethyl pyrimidine moiety of thiamine.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Dougherty, M. and Downs, D.M. The stm4066 gene product of Salmonella enterica serovar Typhimurium has aminoimidazole riboside (AIRs) kinase activity and allows AIRs to satisfy the thiamine requirement of pur mutant strains. J. Bacteriol. 185 (2003) 332-339. [PMID: 12486071]
2. Zhang, Y., Dougherty, M., Downs, D.M. and Ealick, S.E. Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: implications for the evolution of the ribokinase superfamily. Structure 12 (2004) 1809-1821. [PMID: 15458630]
Accepted name: cytidine diphosphoramidate kinase
Reaction: ATP + cytidine 5'-diphosphoramidate = ADP + cytidine 3'-phospho-5'-diphosphoramidate
Systematic name: ATP:cytidine 5'-diphosphoramidate 3'-phosphotransferase
Comments: The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium's capsular polysaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Taylor, Z.W. and Raushel, F.M. Cytidine diphosphoramidate kinase: an enzyme required for the biosynthesis of the O-methyl phosphoramidate modification in the capsular polysaccharides of Campylobacter jejuni. Biochemistry 57 (2018) 2238-2244. [PMID: 29578334]
Accepted name: L-serine kinase (ATP)
Reaction: ATP + L-serine = ADP + O-phospho-L-serine
For diagram of reaction click here.
Other name(s): sbnI (gene name)
Systematic name: ATP:L-serine 3-phosphotransferase
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of L-2,3-diaminopropanoate, which is used by that organism as a precursor for the biosynthesis of the siderophore staphyloferrin B.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Verstraete, M.M., Perez-Borrajero, C., Brown, K.L., Heinrichs, D.E. and Murphy, M.EP. SbnI is a free serine kinase that generates O -phospho-l-serine for staphyloferrin B biosynthesis in Staphylococcus aureus. J. Biol. Chem 293 (2018) 6147-6160. [PMID: 29483190]
Accepted name: L-serine kinase (ADP)
Reaction: ADP + L-serine = AMP + O-phospho-L-serine
Other name(s): serK (gene name)
Systematic name: ADP:L-serine 3-phosphotransferase
Comments: The enzyme, characterized in the hyperthermophilic archaeon Thermococcus kodakarensis, participates in L-cysteine biosynthesis.
Links to other databases: BRENDA, EXPASY, ExplorEnz, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Makino, Y., Sato, T., Kawamura, H., Hachisuka, S.I., Takeno, R., Imanaka, T. and Atomi, H. An archaeal ADP-dependent serine kinase involved in cysteine biosynthesis and serine metabolism. Nat Commun 7 (2016) 13446. [PMID: 27857065]
2. Nagata, R., Fujihashi, M., Kawamura, H., Sato, T., Fujita, T., Atomi, H. and Miki, K. Structural study on the reaction mechanism of a free serine kinase involved in cysteine biosynthesis. ACS Chem. Biol. 12 (2017) 1514-1523. [PMID: 28358477]
Accepted name: inositol phosphorylceramide synthase
Reaction: 1-phosphatidyl-1D-myo-inositol + a very-long-chain (2'R)-2'-hydroxy-phytocermide = 1,2-diacyl-sn-glycerol + a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide
Glossary: a very-long-chain inositol phospho-(2'R)-2'-hydroxyphytoceramide = a very-long-chain inositol phospho-α-hydroxyphytoceramide = IPC
Other name(s): AUR1 (gene name); KEI1 (gene name)
Systematic name: 1-phosphatidyl-1D-myo-inositol:(2'R)-2'-hydroxy-phytoceramide phosphoinositoltransferase
Comments: The enzyme, characterized from yeast, attaches a phosphoinositol headgroup to α-hydroxyphytoceramides, generating a very-long-chain inositol phospho-α hydroxyphytoceramide (IPC), the simplest of the three complex sphingolipids produced by yeast.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Nagiec, M.M., Nagiec, E.E., Baltisberger, J.A., Wells, G.B., Lester, R.L. and Dickson, R.C. Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J. Biol. Chem 272 (1997) 9809-9817. [PMID: 9092515]
2. Levine, T.P., Wiggins, C.A. and Munro, S. Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae. Mol. Biol. Cell 11 (2000) 2267-2281. [PMID: 10888667]
3. Sato, K., Noda, Y. and Yoda, K. Kei1: a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization. Mol. Biol. Cell 20 (2009) 4444-4457. [PMID: 19726565]
Accepted name: mannosyl-inositol-phosphoceramide inositolphosphotransferase
Reaction: 1-phosphatidyl-1D-myo-inositol + a very-long-chain mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide = 1,2-diacyl-sn-glycerol + a very-long-chain mannosyl-diphosphoinositol-(2'R)-2'-hydroxyphytoceramide
Glossary: a very-long-chain mannosyl-diphosphoinositol-(2'R)-2'-hydroxyphytoceramide = a very-long-chain mannosyl-diphosphoinositol-α-hydroxyphytoceramide = MIP2C
Other name(s): IPT1 (gene name)
Systematic name: 1-phosphatidyl-1D-myo-inositol:mannosylinositol phospho-(2'R)-2'-hydroxyphytoceramide phosphoinositoltransferase
Comments: This enzyme catalyses the ultimate reaction in the yeast sphingolipid biosynthesis pathway. It transfers a second phosphoinositol group to mannosyl-inositol-phospho-α-hydroxyphytoceramide (MIPC), forming the final and most abundant yeast sphingolipid, mannosyl-diphosphoinositol-ceramide (MIP2C).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Dickson, R.C., Nagiec, E.E., Wells, G.B., Nagiec, M.M. and Lester, R.L. Synthesis of mannose-(inositol-P)2-ceramide, the major sphingolipid in Saccharomyces cerevisiae, requires the IPT1 (YDR072c) gene. J. Biol. Chem 272 (1997) 29620-29625. [PMID: 9368028]
Accepted name: deoxyribokinase
Reaction: ATP + 2-deoxy-D-ribose = ADP + 2-deoxy-D-ribose 5-phosphate
Other name(s): deoK (gene name)
Systematic name: ATP:2-deoxy-D-ribose 5-phosphotransferase
Comments: The enzyme, characterized from bacteria, is much more active with 2-deoxy-D-ribose than with D-ribose. cf. EC 2.7.1.15, ribokinase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Domagk, G.F. and Horecker, B.L. Pentose fermentation by Lactobacillus plantarum. V. Fermentation of 2-deoxy-D-ribose. J. Biol. Chem 233 (1958) 283-286. [PMID: 13563487]
2. Ginsburg, A. A deoxyribokinase from Lactobacillus plantarum. J. Biol. Chem. 234 (1959) 481-487. [PMID: 13641245]
3. Hoffee, P.A. 2-deoxyribose gene-enzyme complex in Salmonella typhimurium. I. Isolation and enzymatic characterization of 2-deoxyribose-negative mutants. J. Bacteriol. 95 (1968) 449-457. [PMID: 4867740]
4. Tourneux, L., Bucurenci, N., Saveanu, C., Kaminski, P.A., Bouzon, M., Pistotnik, E., Namane, A., Marliere, P., Barzu, O., Li De La Sierra, I., Neuhard, J. and Gilles, A.M. Genetic and biochemical characterization of Salmonella enterica serovar Typhi deoxyribokinase. J. Bacteriol. 182 (2000) 869-873. [PMID: 10648508]
Accepted name: amicoumacin kinase
Reaction: ATP + amicoumacin A = ADP + amicoumacin A 2-phosphate
Other name(s): amiN (gene name); yerI (gene name)
Systematic name: ATP:amicoumacin A 2-phosphotransferase
Comments: The enzyme, found in some bacterial species, inactivates the antibiotic amicoumacin A by phosphorylating it, conferring resistance on the bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Terekhov, S.S., Smirnov, I.V., Malakhova, M.V., Samoilov, A.E., Manolov, A.I., Nazarov, A.S., Danilov, D.V., Dubiley, S.A., Osterman, I.A., Rubtsova, M.P., Kostryukova, E.S., Ziganshin, R.H., Kornienko, M.A., Vanyushkina, A.A., Bukato, O.N., Ilina, E.N., Vlasov, V.V., Severinov, K.V., Gabibov, A.G. and Altman, S. Ultrahigh-throughput functional profiling of microbiota communities. Proc. Natl Acad. Sci. USA 115 (2018) 9551-9556. [PMID: 30181282]
Accepted name: 3-oxoisoapionate kinase
Reaction: ATP + 3-oxoisoapionate = ADP + 3-oxoisoapionate 4-phosphate
Glossary: 3-oxoisoapionate = 2,4-dihydroxy-2-(hydroxymethyl)-3-oxobutanoate
Other name(s): oiaK (gene name)
Systematic name: ATP:3-oxoisoapionate 4-phosphotransferase
Comments: The enzyme, characterized from several bacterial species, participates in the degradation of D-apionate. Stereospecificity of the product, 3-oxoisoapionate 4-phosphate, has not been determined.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Carter, M.S., Zhang, X., Huang, H., Bouvier, J.T., Francisco, B.S., Vetting, M.W., Al-Obaidi, N., Bonanno, J.B., Ghosh, A., Zallot, R.G., Andersen, H.M., Almo, S.C. and Gerlt, J.A. Functional assignment of multiple catabolic pathways for D-apiose. Nat. Chem. Biol. 14 (2018) 696-705. [PMID: 29867142]
Accepted name: levoglucosan kinase
Reaction: ATP + levoglucosan + H2O = ADP + D-glucose 6-phosphate
Glossary: levoglucosan = 1,6-anhydro-β-D-glucopyranose
Systematic name: ATP:1,6-anhydro-β-D-glucopyranose 6-phosphotransferase (hydrolyzing)
Comments: Levoglucosan is formed from the pyrolysis of carbohydrates such as starch and cellulose and is an important molecular marker for pollution from biomass burning. The enzyme, found in yeast and fungi, requires a magnesium ion. cf. EC 1.1.1.425, levoglucosan dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Zhuang, X. and Zhang, H. Identification, characterization of levoglucosan kinase, and cloning and expression of levoglucosan kinase cDNA from Aspergillus niger CBX-209 in Escherichia coli. Protein Expr. Purif. 26 (2002) 71-81. [PMID: 12356473]
2. Dai, J., Yu, Z., He, Y., Zhang, L., Bai, Z., Dong, Z., Du, Y. and Zhang, H. Cloning of a novel levoglucosan kinase gene from Lipomyces starkeyi and its expression in Escherichia coli. World J. Microbiol. Biotechnol. 25 (2009) 1589-1595.
3. Layton, D.S., Ajjarapu, A., Choi, D.W. and Jarboe, L.R. Engineering ethanologenic Escherichia coli for levoglucosan utilization. Bioresour. Technol. 102 (2011) 8318-8322. [PMID: 21719279]
4. Islam, Z.U., Zhisheng, Y., Hassan el, B., Dongdong, C. and Hongxun, Z. Microbial conversion of pyrolytic products to biofuels: a novel and sustainable approach toward second-generation biofuels. J. Ind. Microbiol. Biotechnol. 42 (2015) 1557-1579. [PMID: 26433384]
5. Bacik, J.P., Klesmith, J.R., Whitehead, T.A., Jarboe, L.R., Unkefer, C.J., Mark, B.L. and Michalczyk, R. Producing glucose 6-phosphate from cellulosic biomass: structural insights into levoglucosan bioconversion. J. Biol. Chem. 290 (2015) 26638-26648. [PMID: 26354439]
Accepted name: apulose kinase
Reaction: ATP + apulose = ADP + apulose 4-phosphate
Glossary: apulose = 1,3,4-trihydroxy-3-(hydroxymethyl)butan-2-one
Other name(s): aplK (gene name)
Systematic name: ATP:apulose 4-phosphotransferase
Comments: The enzyme, characterized from several bacterial species, is involved in a catabolic pathway for D-apiose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Carter, M.S., Zhang, X., Huang, H., Bouvier, J.T., Francisco, B.S., Vetting, M.W., Al-Obaidi, N., Bonanno, J.B., Ghosh, A., Zallot, R.G., Andersen, H.M., Almo, S.C. and Gerlt, J.A. Functional assignment of multiple catabolic pathways for D-apiose. Nat. Chem. Biol. 14 (2018) 696-705. [PMID: 29867142]
Accepted name: D-tagatose-1-phosphate kinase
Reaction: ATP + D-tagatopyranose 1-phosphate = ADP + D-tagatopyranose 1,6-bisphosphate
Other name(s): TagK
Systematic name: ATP:D-tagatose-1-phosphate 6-phosphotransferase
Comments: The enzyme, which has been purified from the bacteria Klebsiella oxytoca and Bacillus licheniformis, is part of a D-tagatose catabolic pathway. The substrate, which occurs in a pyranose form in solution, undergoes a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Van der Heiden, E., Delmarcelle, M., Simon, P., Counson, M., Galleni, M., Freedberg, D.I., Thompson, J., Joris, B. and Battistel, M.D. Synthesis and physicochemical characterization of D-tagatose-1-phosphate: the substrate of the tagatose-1-phosphate kinase in the phosphotransferase system-mediated D-tagatose catabolic pathway of Bacillus licheniformis, J. Mol. Microbiol. Biotechnol. 25 (2015) 106-119. [PMID: 26159072]
Accepted name: lipopolysaccharide core heptose(I) kinase
Reaction: ATP + an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] = ADP + an α-Hep-(1→3)-4-O-phospho-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A]
Glossary: Lipid A is a lipid component of the lipopolysaccharides (LPS) of Gram-negative bacteria. It usually consists of two glucosamine units connected by a β(1→6) bond and decorated with four to seven acyl chains and up to two phosphate groups.
Hep = L-glycero-β-D-manno-heptose.
Other name(s): WaaP; RfaP
Systematic name: ATP:an α-Hep-(1→3)-α-Hep-(1→5)-[α-Kdo-(2→4)]-α-Kdo-(2→6)-[lipid A] heptoseI 4-O-phosphotransferase
Comments: The enzyme catalyses the phosphorylation of L-glycero-D-manno-heptose I (the first heptose added to the lipid, Hep I) in the biosynthesis of the inner core oligosaccharide of the lipopolysaccharide (endotoxin) of some Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Yethon, J.A. and Whitfield, C. Purification and characterization of WaaP from Escherichia coli, a lipopolysaccharide kinase essential for outer membrane stability. J. Biol. Chem. 276 (2001) 5498-5504. [PMID: 11069912]
2. Zhao, X. and Lam, J.S. WaaP of Pseudomonas aeruginosa is a novel eukaryotic type protein-tyrosine kinase as well as a sugar kinase essential for the biosynthesis of core lipopolysaccharide. J. Biol. Chem. 277 (2002) 4722-4730. [PMID: 11741974]
3. Kreamer, N.NK., Chopra, R., Caughlan, R.E., Fabbro, D., Fang, E., Gee, P., Hunt, I., Li, M., Leon, B.C., Muller, L., Vash, B., Woods, A.L., Stams, T., Dean, C.R. and Uehara, T. Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase. Sci. Rep. 8 (2018) 14124. [PMID: 30237436]
Accepted name: NAD+ 3'-kinase
Reaction: ATP + NAD+ = ADP + 3'-NADP+
Glossary: 3'-NADP = nicotinamide adenine dinucleotide 3'-phosphate
Other name(s): AvrRxo1
Systematic name: ATP:NAD+ 3'-phosphotransferase
Comments: The enzyme, best characterized from the plant pathogenic bacterium Xanthomonas oryzae pv. oryzicola, is considered a bacterial type III effector. The product, 3'-NADP, is believed to enhance bacterial virulence on plants through manipulation of primary metabolic pathways. In vitro the enzyme is also active with nicotinate adenine dinucleotide (deamido-NAD).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Schuebel, F., Rocker, A., Edelmann, D., Schessner, J., Brieke, C. and Meinhart, A. 3'-NADP and 3'-NAADP, Two Metabolites Formed by the Bacterial Type III Effector AvrRxo1. J. Biol. Chem. 291 (2016) 22868-22880. [PMID: 27621317]
2. Shidore, T., Broeckling, C.D., Kirkwood, J.S., Long, J.J., Miao, J., Zhao, B., Leach, J.E. and Triplett, L.R. The effector AvrRxo1 phosphorylates NAD in planta. PLoS Pathog. 13 (2017) e1006442. [PMID: 28628666]
Accepted name: GTP-dependent dephospho-CoA kinase
Reaction: GTP + 3'-dephospho-CoA = GDP + CoA
Systematic name: GTP:3'-dephospho-CoA 3'-phosphotransferase
Comments: The enzyme, characterized from the archaeon Thermococcus kodakarensis, participates in a coenzyme A biosynthesis pathway. cf. EC 2.7.1.24, dephospho-CoA kinase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number:
References:
1. Shimosaka, T., Makarova, K.S., Koonin, E.V. and Atomi, H. Identification of dephospho-coenzyme A (dephospho-CoA) kinase in Thermococcus kodakarensis and elucidation of the entire CoA biosynthesis pathway in archaea. mBio 10 (2019) . [PMID: 31337720]
Accepted name: phenol phosphorylase
Reaction: ATP + phenol + H2O = AMP + phenyl phosphate + phosphate
Other name(s): phenylphosphate synthase
Systematic name: ATP:phenol phosphotransferase (AMP-forming)
Comments: The enzyme, characterized from the bacterium Thauera aromatica, catalyses the first step in an anaerobic phenol degradation pathway. The enzyme, composed of three subunits, transfers the β-phosphoryl from ATP to phenol, forming phenyl phosphate, AMP, and phosphate [1]. During catalysis a diphosphoryl group is transferred from ATP to a histidine residue in one of the enzyme's subunits, from which phosphate is cleaved to render the reaction unidirectional. The remaining histidine phosphate subsequently serves as the actual phosphorylation agent [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Schmeling, S., Narmandakh, A., Schmitt, O., Gad'on, N., Schuhle, K. and Fuchs, G. Phenylphosphate synthase: a new phosphotransferase catalyzing the first step in anaerobic phenol metabolism in Thauera aromatica. J. Bacteriol. 186 (2004) 8044-8057. [PMID: 15547277]
2. Narmandakh, A., Gad'on, N., Drepper, F., Knapp, B., Haehnel, W. and Fuchs, G. Phosphorylation of phenol by phenylphosphate synthase: role of histidine phosphate in catalysis. J. Bacteriol. 188 (2006) 7815-7822. [PMID: 16980461]
Accepted name: α-D-ribose-1-phosphate 5-kinase (ATP)
Reaction: ATP + α-D-ribose-1-phosphate = ADP + α-D-ribose 1,5-bisphosphate
Systematic name: ATP:α-D-ribose-1-phosphate 5-phosphotransferase
Comments: The enzyme, characterized from the halophilic archaeon Halopiger xanaduensis, participates in a non-carboxylating pentose bisphosphate pathway for nucleoside degradation, which is found in some halophilic archaea. cf. EC 2.7.1.212, α-D-ribose-1-phosphate 5-kinase (ADP).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Sato, T., Utashima, S.H., Yoshii, Y., Hirata, K., Kanda, S., Onoda, Y., Jin, J.Q., Xiao, S., Minami, R., Fukushima, H., Noguchi, A., Manabe, Y., Fukase, K. and Atomi, H. A non-carboxylating pentose bisphosphate pathway in halophilic archaea. Commun Biol 5 (2022) 1290. [PMID: 36434094]