EC 2.7.7 (continued)

Continued from:

EC 2.7.7.1 to EC 2.7.7.50

Contents

Entries

Accepted name: adenylylsulfate—ammonia adenylyltransferase

Reaction: adenylyl sulfate + NH₃ = adenosine 5'-phosphoramidate + sulfate

Other names: APSAT; adenylylsulfate:ammonia adenylyltransferase

Systematic name: adenylyl-sulfate:ammonia adenylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 79121-94-1

References:

1. Fankhauser, H., Schiff, J.A. and Garber, L.J. Purification and properties of adenylyl sulphate:ammonia adenylyltransferase from Chlorella catalysing the formation of adenosine 5′ -phosphoramidate from adenosine 5′ -phosphosulphate and ammonia. 195 (1981) 545–560. [PMID: 6274307]

EC 2.7.7.52

Accepted name: RNA uridylyltransferase

Reaction: UTP + RNA_n = diphosphate + RNA_n+1

Other name(s): terminal uridylyltransferase; TUT

Systematic name: UTP:RNA uridylyltransferase

Comments: The enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 78519-53-6

References:

1. Zabel, P., Dorssers, L., Wernars, K. and van Kammen, A. Terminal uridylyl transferase of Vigna unguiculata: purification and characterization of an enzyme catalyzing the addition of a single UMP residue to the 3'-end of an RNA primer. Nucleic Acids Res. 9 (1981) 2433-2453. [PMID: 6269049]

EC 2.7.7.53

Accepted name: ATP adenylyltransferase

Reaction: ADP + ATP = phosphate + P¹,P⁴-bis(5'-adenosyl) tetraphosphate

Other name(s): bis(5'-nucleosyl)-tetraphosphate phosphorylase (NDP-forming); diadenosinetetraphosphate αβ-phosphorylase; adenine triphosphate adenylyltransferase; diadenosine 5',5'"-P¹,P⁴-tetraphosphate αβ-phosphorylase (ADP-forming); dinucleoside oligophosphate αβ-phosphorylase

Systematic name: ADP:ATP adenylyltransferase

Comments: GTP and adenosine tetraphosphate can also act as adenylyl acceptors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 96697-71-1

References:

1. Guranowski, A. and Blanquet, S. Phosphorolytic cleavage of diadenosine 5',5'''-P¹,P⁴-tetraphosphate. Properties of homogeneous diadenosine 5',5'''- P¹,P⁴-tetraphosphate αβ-phosphorylase from Saccharomyces cerevisiae. J. Biol. Chem. 260 (1985) 3542-3547. [PMID: 2982863]

[EC 2.7.7.54 Deleted entry: phenylalanine adenylyltransferase. The activity is part of EC 6.3.2.40, cyclopeptine synthase. (EC 2.7.7.54 created 1989, deleted 2013)]

[EC 2.7.7.55 Deleted entry: anthranilate adenylyltransferase. The activity is part of EC 6.3.2.40, cyclopeptine synthase. (EC 2.7.7.55 created 1989, deleted 2013)]

EC 2.7.7.56

Accepted name: tRNA nucleotidyltransferase

Reaction: tRNA_n+1 + phosphate = tRNA_n + a nucleoside diphosphate

Other name(s): phosphate-dependent exonuclease; RNase PH; ribonuclease PH

Systematic name: tRNA:phosphate nucleotidyltransferase

Comments: Brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate. Not identical with EC 2.7.7.8 polyribonucleotide nucleotidyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 116412-36-3

References:

1. Cudny, H. and Deutscher, M.P. 3' processing of tRNA precursors in ribonuclease-deficient Escherichia coli. Development and characterization of an in vitro processing system and evidence for a phosphate requirement. J. Biol. Chem. 263 (1988) 1518-1523. [PMID: 3275667]

2. Deutscher, M.P., Marshall, G.T. and Cudny, H. RNase PH: an Escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase. Proc. Natl. Acad. Sci. USA 85 (1988) 4710-4714. [PMID: 2455297]

EC 2.7.7.57

Accepted name: N-methylphosphoethanolamine cytidylyltransferase

Reaction: CTP + N-methylethanolamine phosphate = diphosphate + CDP-N-methylethanolamine

Other names: monomethylethanolamine phosphate cytidylyltransferase; CTP:P-MEA cytidylyltransferase

Systematic name: CTP:N-methylethanolamine-phosphate cytidylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 119345-28-7

References:

1. Datko, A.H. and Mudd, S.H. Enzymes of phosphatidylcholine synthesis in Lemna, soybean, and carrot. Plant Physiol. 88 (1988) 1338-1348.

EC 2.7.7.58

Transferred entry: (2,3-dihydroxybenzoyl)adenylate synthase. Now included in EC 6.2.1.71, 2,3-dihydroxybenzoate[aryl-carrier protein] ligase

EC 2.7.7.59

Accepted name: [protein-PII] uridylyltransferase

Reaction: UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]

Other name(s): PII uridylyl-transferase; uridyl removing enzyme

Systematic name: UTP:[protein-PII] uridylyltransferase

Comments: the enzyme uridylylates and de-uridylylates the small trimeric protein PII. The enzymes from Escherichia coli and Salmonella typhimurium have been wrongly identified, in some databases, as EC 2.7.7.12 (UDP-glucose—hexose-1-phosphate uridylyltransferase), from which it differs greatly in both reaction catalysed and sequence.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 57657-57-5

References:

1. Garcia, E., Rhee, S.G. Cascade control of Escherichia coli glutamate synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme. J. Biol. Chem. 258 (1983) 2246-2253. [PMID: 6130097]

2. Van Heeswijk, W., Rabenberg, M., Westerhoff, H., Kahn, D. The genes of the glutamate synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli. Mol. Microbiol. 9 (1993) 443-457. [PMID: 8412694]

EC 2.7.7.60

Accepted name: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Reaction: CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol

For diagram click here.

Other name(s): MEP cytidylyltransferase

Systematic name: CTP:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase

Comments: The enzyme from Escherichia coli requires Mg²⁺ or Mn²⁺. ATP or UTP can replace CTP, but both are less effective. GTP and TTP are not substrates. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 251990-59-7

References:

1. Rohdich, F., Wungsintaweekul, J., Fellermeier, M., Sagner, S., Herz, S., Kis, K., Eisenreich, W., Bacher, A. and Zenk, M.H. Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erithritol. Proc. Natl. Acad. Sci. USA 96 (1999) 11758-11763. [PMID: 10518523]

2. Kuzuyama, T., Takagi, M., Kaneda, K., Dairi, T. and Seto, H. Formation of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate pathway. Tetrahedron Lett. 41 (2000) 703-706.

EC 2.7.7.61

Accepted name: citrate lyase holo-[acyl-carrier protein] synthase

Reaction: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + apo-[citrate (pro-3S)-lyase] = diphosphate + holo-[citrate (pro-3S)-lyase]

For diagram of reaction, click here

Other name(s): 2'-(5''-phosphoribosyl)-3'-dephospho-CoA transferase; 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase; CitX; holo-ACP synthase (ambiguous); 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase adenylyltransferase; 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA transferase; 2'-(5''-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate-lyase adenylyltransferase; holo-citrate lyase synthase (incorrect); 2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate-lyase 2'-(5-phosphoribosyl)-3'-dephospho-CoA-transferase

Systematic name: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-[citrate (pro-3S)-lyase] 2'-(5-phosphoribosyl)-3'-dephospho-CoA-transferase

Comments: The γ-subunit of EC 4.1.3.6, citrate (pro-3S) lyase, serves as an acyl-carrier protein (ACP) and contains the cofactor 2'-(5-triphosphoribosyl)-3'-dephospho-CoA [1,3]. Synthesis and attachment of the cofactor requires the concerted action of this enzyme and EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase [1]. In the enzyme from Escherichia coli, the cofactor is attached to serine-14 of the ACP via a phosphodiester bond.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 312492-44-7

References:

1. Schneider, K., Dimroth, P. and Bott, M. Biosynthesis of the prosthetic group of citrate lyase. Biochemistry 39 (2000) 9438-9450. [PMID: 10924139]

2. Schneider, K., Dimroth, P. and Bott, M. Identification of triphosphoribosyl-dephospho-CoA as precursor of the citrate lyase prosthetic group. FEBS Lett. 483 (2000) 165-168. [PMID: 11042274]

3. Schneider, K., Kästner, C.N., Meyer, M., Wessel, M., Dimroth, P. and Bott, M. Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group. J. Bacteriol. 184 (2002) 2439-2446. [PMID: 11948157]

EC 2.7.7.62

Accepted name: adenosylcobinamide-phosphate guanylyltransferase

Reaction: GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide-GDP

For diagram click here.

Other name(s): CobU; adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase; AdoCbi kinase/AdoCbi-phosphate guanylyltransferase

Systematic name: GTP:adenosylcobinamide-phosphate guanylyltransferase

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 nuclotide loop assembly pathway is the cobinamide (Cbi) activation branch where AdoCbi or adenosylcobinamide-phosphate is converted to the activated intermediate AdoCbi-GDP by the bifunctional enzyme 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, cobalamin synthase (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) 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]. The guanylyltransferase reaction is a two-stage reaction with formation of a CobU-GMP intermediate [1]. Guanylylation takes place at histidine-46.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 169592-55-6

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]

[EC 2.7.7.63 Transferred entry: lipoate—protein ligase, now EC EC 6.3.1.20, lipoate—protein ligase. (EC 2.7.7.63 created 2006, deleted 2016)]

EC 2.7.7.64

Accepted name: UTP-monosaccharide-1-phosphate uridylyltransferase

Reaction: UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide

Glossary: UDP-Xyl = UDP-α-D-xylose
UDP-L-Ara = UDP-β-L-arabinopyranose

Other name(s): UDP-sugar pyrophosphorylase; PsUSP

Comments: Requires Mg²⁺ or Mn²⁺ for maximal activity. The reaction can occur in either direction and it has been postulated that MgUTP and Mg-diphosphate are the actual substrates [1,2]. The enzyme catalyses the formation of UDP-Glc, UDP-Gal, UDP-GlcA, UDP-L-Ara and UDP-Xyl, showing broad substrate specificity towards monosaccharide 1-phosphates. Mannose 1-phosphate, L-fucose 1-phosphate and glucose 6-phosphate are not substrates and UTP cannot be replaced by other nucleotide triphosphates [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Kotake, T., Yamaguchi, D., Ohzono, H., Hojo, S., Kaneko, S., Ishida, H.K. and Tsumuraya, Y. UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts. J. Biol. Chem. 279 (2004) 45728-45736. [PMID: 15326166]

2. Rudick, V.L. and Weisman, R.A. Uridine diphosphate glucose pyrophosphorylase of Acanthamoeba castellanii. Purification, kinetic, and developmental studies. J. Biol. Chem. 249 (1974) 7832-7840. [PMID: 4430676]

EC 2.7.7.65

Accepted name: diguanylate cyclase

Reaction: 2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate

For diagram of reaction click here

Glossary: c-di-GMP = c-di-guanylate = cyclic di-3',5'-guanylate = cyclic-bis(3'→5') dimeric GMP

Other name(s): DGC; PleD

Systematic name: GTP:GTP guanylyltransferase (cyclizing)

Comments: A GGDEF-domain-containing protein that requires Mg²⁺ or Mn²⁺ for activity. The enzyme can be activated by BeF₃, a phosphoryl mimic, which results in dimerization [3]. Dimerization is required but is not sufficient for diguanylate-cyclase activity [3]. Cyclic di-3',5'-guanylate is an intracellular signalling molecule that controls motility and adhesion in bacterial cells. It was first identified as having a positive allosteric effect on EC 2.4.1.12, cellulose synthase (UDP-forming) [1].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Ryjenkov, D.A., Tarutina, M., Moskvin, O.V. and Gomelsky, M. Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J. Bacteriol. 187 (2005) 1792-1798. [PMID: 15716451]

2. Méndez-Ortiz, M.M., Hyodo, M., Hayakawa, Y. and Membrillo-Hernández, J. Genome-wide transcriptional profile of Escherichia coli in response to high levels of the second messenger 3',5'-cyclic diguanylic acid. J. Biol. Chem. 281 (2006) 8090-8099. [PMID: 16418169]

3. Paul, R., Abel, S., Wassmann, P., Beck, A., Heerklotz, H. and Jenal, U. Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization. J. Biol. Chem. 282 (2007) 29170-29177. [PMID: 17640875]

EC 2.7.7.66

Accepted name: malonate decarboxylase holo-[acyl-carrier protein] synthase

Reaction: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + malonate decarboxylase apo-[acyl-carrier protein] = malonate decarboxylase holo-[acyl-carrier protein] + diphosphate

For diagram click here

Other name(s): holo ACP synthase (ambiguous); 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo ACP 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA transferase; MdcG; 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-malonate-decarboxylase adenylyltransferase; holo-malonate-decarboxylase synthase (incorrect)

Systematic name: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-malonate-decarboxylase 2'-(5-phosphoribosyl)-3'-dephospho-CoA-transferase

Comments: The δ subunit of malonate decarboxylase serves as an an acyl-carrier protein (ACP) and contains the cofactor 2'-(5-triphosphoribosyl)-3'-dephospho-CoA. Two reactions are involved in the production of the holo-ACP form of this enzyme. The first reaction is catalysed by EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase. The resulting prosthetic group is then attached to the ACP subunit via a phosphodiester linkage to a serine residue, thus forming the holo form of the enzyme, in a manner analogous to that of EC 2.7.7.61, citrate lyase holo-[acyl-carrier protein] synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hoenke, S., Wild, M.R. and Dimroth, P. Biosynthesis of triphosphoribosyl-dephospho-coenzyme A, the precursor of the prosthetic group of malonate decarboxylase. Biochemistry 39 (2000) 13223-13232. [PMID: 11052675]

2. Hoenke, S., Schmid, M. and Dimroth, P. Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases. Biochemistry 39 (2000) 13233-13240. [PMID: 11052676]

EC 2.7.7.67

Accepted name: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase

Reaction: CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol

For diagram of reaction click here.

Glossary: 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate = 2,3-bis-(O-geranylgeranyl)-glycerophosphate ether = unsaturated archaetidic acid
CDP-unsaturated archaeol = CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol

Other name(s): carS (gene name); CDP-2,3-di-O-geranylgeranyl-sn-glycerol synthase; CTP:2,3-GG-GP ether cytidylyltransferase; CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase; CDP-2,3-bis-O-(geranylgeranyl)-sn-glycerol synthase; CTP:2,3-bis-O-(geranylgeranyl)-sn-glycero-1-phosphate cytidylyltransferase; CDP-unsaturated archaeol synthase; CDP-archaeol synthase (incorrect)

Systematic name: CTP:2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate cytidylyltransferase

Comments: This enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes [1]. The enzyme requires Mg²⁺ and K⁺ for maximal activity [1].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 329791-09-5

References:

1. Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568-36574. [PMID: 10960477]

2. Morii, H. and Koga, Y. CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. J. Bacteriol. 185 (2003) 1181-1189. [PMID: 12562787]

3. Jain, S., Caforio, A., Fodran, P., Lolkema, J.S., Minnaard, A.J. and Driessen, A.J. Identification of CDP-archaeol synthase, a missing link of ether lipid biosynthesis in Archaea. Chem. Biol. 21 (2014) 1392-1401. [PMID: 25219966]

EC 2.7.7.68

Accepted name: 2-phospho-L-lactate guanylyltransferase

Reaction: (2S)-2-phospholactate + GTP = (2S)-lactyl-2-diphospho-5'-guanosine + diphosphate

For diagram of coenzyme F₄₂₀ biosynthesis, click here

Other name(s): cofC (gene name) (ambiguous)

Systematic name: GTP:2-phospho-L-lactate guanylyltransferase

Comments: This enzyme is involved in the biosynthesis of coenzyme F₄₂₀, a redox-active cofactor, in all methanogenic archaea. cf. EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase and EC 2.7.7.106, 3-phospho-(R)-glycerate guanylyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc PDB, CAS registry number:

References:

1. Grochowski, L.L., Xu, H. and White, R.H. Identification and characterization of the 2-phospho-L-lactate guanylyltransferase involved in coenzyme F₄₂₀ biosynthesis. Biochemistry 47 (2008) 3033-3037. [PMID: 18260642]

2. Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088-2094. [PMID: 31469543]

EC 2.7.7.69

Accepted name: GDP-L-galactose/GDP-D-glucose: hexose 1-phosphate guanylyltransferase

Reaction: (1) GDP-β-L-galactose + α-D-mannose 1-phosphate = β-L-galactose 1-phosphate + GDP-α-D-mannose
(2) GDP-α-D-glucose + α-D-mannose 1-phosphate = α-D-glucose 1-phosphate + GDP-α-D-mannose

Other name(s): VTC2; VTC5; GDP-L-galactose phosphorylase

Systematic name: GDP-β-L-galactose/GDP-α-D-glucose:hexose 1-phosphate guanylyltransferase

Comments: This plant enzyme catalyses the conversion of GDP-β-L-galactose and GDP-α-D-glucose to β-L-galactose 1-phosphate and α-D-glucose 1-phosphate, respectively. The enzyme can use inorganic phosphate as the co-substrate, but several hexose 1-phosphates, including α-D-mannose 1-phosphate, α-D-glucose 1-phosphate, and α-D-galactose 1-phosphate, are better guanylyl acceptors. The enzyme's activity on GDP-β-L-galactose is crucial for the biosynthesis of L-ascorbate.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Linster, C.L., Gomez, T.A., Christensen, K.C., Adler, L.N., Young, B.D., Brenner, C. and Clarke, S.G. Arabidopsis VTC2 encodes a GDP-L-galactose phosphorylase, the last unknown enzyme in the Smirnoff-Wheeler pathway to ascorbic acid in plants. J. Biol. Chem. 282 (2007) 18879-18885. [PMID: 17462988]

2. Dowdle, J., Ishikawa, T., Gatzek, S., Rolinski, S. and Smirnoff, N. Two genes in Arabidopsis thaliana encoding GDP-L-galactose phosphorylase are required for ascorbate biosynthesis and seedling viability. Plant J. 52 (2007) 673-689. [PMID: 17877701]

3. Wolucka, B.A. and Van Montagu, M. The VTC2 cycle and the de novo biosynthesis pathways for vitamin C in plants: an opinion. Phytochemistry 68 (2007) 2602-2613. [PMID: 17950389]

4. Laing, W.A., Wright, M.A., Cooney, J. and Bulley, S.M. The missing step of the L-galactose pathway of ascorbate biosynthesis in plants, an L-galactose guanyltransferase, increases leaf ascorbate content. Proc. Natl. Acad. Sci. USA 104 (2007) 9534-9539. [PMID: 17485667]

5. Linster, C.L., Adler, L.N., Webb, K., Christensen, K.C., Brenner, C. and Clarke, S.G. A second GDP-L-galactose phosphorylase in arabidopsis en route to vitamin C. Covalent intermediate and substrate requirements for the conserved reaction. J. Biol. Chem. 283 (2008) 18483-18492. [PMID: 18463094]

6. Muller-Moule, P. An expression analysis of the ascorbate biosynthesis enzyme VTC2. Plant Mol. Biol. 68 (2008) 31-41. [PMID: 18516687]

EC 2.7.7.70

Accepted name: D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase

Reaction: D-glycero-β-D-manno-heptose 1-phosphate + ATP = ADP-D-glycero-β-D-manno-heptose + diphosphate

Other name(s): D-β-D-heptose 7-phosphate kinase/D-β-D-heptose 1-phosphate adenylyltransferase; D-glycero-D-manno-heptose-1β-phosphate adenylyltransferase; hldE (gene name); rfaE (gene name)

Systematic name: ATP:D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase

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 2.7.1.167). 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.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Valvano, M.A., Marolda, C.L., Bittner, M., Glaskin-Clay, M., Simon, T.L. and Klena, J.D. The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose. J. Bacteriol. 182 (2000) 488-497. [PMID: 10629197]

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. 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]

EC 2.7.7.71

Accepted name: D-glycero-α-D-manno-heptose 1-phosphate guanylyltransferase

Reaction: D-glycero-α-D-manno-heptose 1-phosphate + GTP = GDP-D-glycero-α-D-manno-heptose + diphosphate

Other name(s): hddC (gene name); gmhD (gene name)

Systematic name: GTP:D-glycero-α-D-manno-heptose 1-phosphate guanylyltransferase

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 some Gram-positive bacteria.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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]

EC 2.7.7.72

Accepted name: CCA tRNA nucleotidyltransferase

Reaction: (1) a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate (overall reaction)
(1a) a tRNA precursor + CTP = a tRNA with a 3' cytidine end + diphosphate
(1b) a tRNA with a 3' cytidine + CTP = a tRNA with a 3' CC end + diphosphate
(1c) a tRNA with a 3' CC end + ATP = a tRNA with a 3' CCA end + diphosphate

Other name(s): CCA-adding enzyme, tRNA adenylyltransferase, tRNA cytidylyltransferase, tRNA CCA-pyrophosphorylase; tRNA-nucleotidyltransferase; transfer-RNA nucleotidyltransferase; transfer ribonucleic acid nucleotidyl transferase; CTP(ATP):tRNA nucleotidyltransferase; transfer ribonucleate adenylyltransferase; transfer ribonucleate adenyltransferase; transfer RNA adenylyltransferase; transfer ribonucleate nucleotidyltransferase; ATP (CTP):tRNA nucleotidyltransferase; ribonucleic cytidylic cytidylic adenylic pyrophosphorylase; transfer ribonucleic adenylyl (cytidylyl) transferase; transfer ribonucleic-terminal trinucleotide nucleotidyltransferase; transfer ribonucleate cytidylyltransferase; ribonucleic cytidylyltransferase; -C-C-A pyrophosphorylase; tRNA cytidylyltransferase; ATP(CTP)-tRNA nucleotidyltransferase; tRNA adenylyl(cytidylyl)transferase; CTP:tRNA cytidylyltransferase

Systematic name: CTP,CTP,ATP:tRNA cytidylyl,cytidylyl,adenylyltransferase

Comments: The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition [5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Schofield, P. and Williams, K.R. Purification and some properties of Escherichia coli tRNA nucleotidyltransferase. J. Biol. Chem. 252 (1977) 5584-5588. [PMID: 328503]

2. Shi, P.Y., Maizels, N. and Weiner, A.M. CCA addition by tRNA nucleotidyltransferase: polymerization without translocation. EMBO J. 17 (1998) 3197-3206. [PMID: 9606201]

3. Augustin, M.A., Reichert, A.S., Betat, H., Huber, R., Morl, M. and Steegborn, C. Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization. J. Mol. Biol. 328 (2003) 985-994. [PMID: 12729736]

4. Yakunin, A.F., Proudfoot, M., Kuznetsova, E., Savchenko, A., Brown, G., Arrowsmith, C.H. and Edwards, A.M. The HD domain of the Escherichia coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities. J. Biol. Chem. 279 (2004) 36819-36827. [PMID: 15210699]

5. Hou, Y.M. CCA addition to tRNA: implications for tRNA quality control. IUBMB Life 62 (2010) 251-260. [PMID: 20101632]

EC 2.7.7.73

Accepted name: sulfur carrier protein ThiS adenylyltransferase

Reaction: ATP + [ThiS] = diphosphate + adenylyl-[ThiS]

Other name(s): thiF (gene name)

Systematic name: ATP:[ThiS] adenylyltransferase

Comments: Binds Zn²⁺. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine. The enzyme shows significant structural similarity to ubiquitin-activating enzyme [3,4]. In Escherichia coli, but not in Bacillus subtilis, the enzyme forms a cross link from Cys-184 to the ThiS carboxy terminus (the position that is also thiolated) via an acyldisulfide [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Taylor, S.V., Kelleher, N.L., Kinsland, C., Chiu, H.J., Costello, C.A., Backstrom, A.D., McLafferty, F.W. and Begley, T.P. Thiamin biosynthesis in Escherichia coli. Identification of this thiocarboxylate as the immediate sulfur donor in the thiazole formation. J. Biol. Chem. 273 (1998) 16555-16560. [PMID: 9632726]

2. Xi, J., Ge, Y., Kinsland, C., McLafferty, F.W. and Begley, T.P. Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein^--protein conjugate that is functionally analogous to the ubiquitin/E1 complex. Proc. Natl. Acad. Sci. USA 98 (2001) 8513-8518. [PMID: 11438688]

3. Duda, D.M., Walden, H., Sfondouris, J. and Schulman, B.A. Structural analysis of Escherichia coli ThiF. J. Mol. Biol. 349 (2005) 774-786. [PMID: 15896804]

4. Lehmann, C., Begley, T.P. and Ealick, S.E. Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry 45 (2006) 11-19. [PMID: 16388576]

EC 2.7.7.74

Accepted name: 1L-myo-inositol 1-phosphate cytidylyltransferase

Reaction: CTP + 1L-myo-inositol 1-phosphate = diphosphate + CDP-1L-myo-inositol

For diagram of reaction click here.

Glossary: 1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate

Other name(s): CTP:inositol-1-phosphate cytidylyltransferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); IPCT (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); L-myo-inositol-1-phosphate cytidylyltransferase

Systematic name: CTP:1L-myo-inositol 1-phosphate cytidylyltransferase

Comments: In many organisms this activity is catalysed by a bifunctional enzyme. The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3'-phosphate, a widespread organic solute in microorganisms adapted to hot environments.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Rodrigues, M.V., Borges, N., Henriques, M., Lamosa, P., Ventura, R., Fernandes, C., Empadinhas, N., Maycock, C., da Costa, M.S. and Santos, H. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. J. Bacteriol. 189 (2007) 5405-5412. [PMID: 17526717]

EC 2.7.7.75

Accepted name: molybdopterin adenylyltransferase

Reaction: ATP + molybdopterin = diphosphate + adenylyl-molybdopterin

For diagram of reaction click here.

Glossary: molybdopterin = H₂Dtpp-mP = [(5aR,8R,9aR)-2-amino-4-oxo-6,7-bis(sulfanyl)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogen phosphate

Other name(s): MogA; Cnx1 (ambiguous)

Systematic name: ATP:molybdopterin adenylyltransferase

Comments: Catalyses the activation of molybdopterin for molybdenum insertion. In eukaryotes, this reaction is catalysed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1). The reaction requires a divalent cation such as Mg²⁺ or Mn²⁺.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Nichols, J.D. and Rajagopalan, K.V. In vitro molybdenum ligation to molybdopterin using purified components. J. Biol. Chem. 280 (2005) 7817-7822. [PMID: 15632135]

2. Kuper, J., Palmer, T., Mendel, R.R. and Schwarz, G. Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilization. Proc. Natl. Acad. Sci. USA 97 (2000) 6475-6480. [PMID: 10823911]

3. Llamas, A., Mendel, R.R. and Schwarz, G. Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion. J. Biol. Chem. 279 (2004) 55241-55246. [PMID: 15504727]

EC 2.7.7.76

Accepted name: molybdenum cofactor cytidylyltransferase

Reaction: CTP + molybdenum cofactor = diphosphate + cytidylyl molybdenum cofactor

For diagram of reaction click here.

Glossary: molybdenum cofactor = MoCo = MoO₂(OH)Dtpp-mP = {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-bis(sulfanyl-kS)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2^-) phosphate}(dioxo)molybdate

Other name(s): MocA, CTP:molybdopterin cytidylyltransferase, MoCo cytidylyltransferase, Mo-MPT cytidyltransferase

Systematic name: CTP:molybdenum cofactor cytidylyltransferase

Comments: Catalyses the cytidylation of the molybdenum cofactor. This modification occurs only in prokaryotes. Divalent cations such as Mg²⁺ or Mn²⁺ are required for activity. ATP or GTP cannot replace CTP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Neumann, M., Mittelstadt, G., Seduk, F., Iobbi-Nivol, C. and Leimkuhler, S. MocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coli. J. Biol. Chem. 284 (2009) 21891-21898. [PMID: 19542235]

2. Neumann, M., Seduk, F., Iobbi-Nivol, C. and Leimkuhler, S. Molybdopterin dinucleotide biosynthesis in Escherichia coli: Identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides. J. Biol. Chem. 286 (2011) 1400-1408. [PMID: 21081498]

EC 2.7.7.77

Accepted name: molybdenum cofactor guanylyltransferase

Reaction: GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor

For diagram of reaction click here.

Glossary: molybdenum cofactor = MoCo = MoO₂(OH)Dtpp-mP = {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-bis(sulfanyl-κS)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2–) phosphate}(dioxo)molybdate

Other name(s): MobA (gene name); MoCo guanylyltransferase

Systematic name: GTP:molybdenum cofactor guanylyltransferase

Comments: Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Lake, M.W., Temple, C.A., Rajagopalan, K.V. and Schindelin, H. The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis. J. Biol. Chem. 275 (2000) 40211-40217. [PMID: 10978347]

2. Temple, C.A. and Rajagopalan, K.V. Mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J. Biol. Chem. 275 (2000) 40202-40210. [PMID: 10978348]

3. Guse, A., Stevenson, C.E., Kuper, J., Buchanan, G., Schwarz, G., Giordano, G., Magalon, A., Mendel, R.R., Lawson, D.M. and Palmer, T. Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA. J. Biol. Chem. 278 (2003) 25302-25307. [PMID: 12719427]

EC 2.7.7.78

Accepted name: GDP-D-glucose phosphorylase

Reaction: GDP-α-D-glucose + phosphate = α-D-glucose 1-phosphate + GDP

Systematic name: GDP:α-D-glucose 1-phosphate guanylyltransferase

Comments: The enzyme may be involved in prevention of misincorporation of glucose in place of mannose residues into glycoconjugates i.e. to remove accidentally produced GDP-α-D-glucose. Activities with GDP-L-galactose, GDP-D-mannose and UDP-D-glucose are all less than 3% that with GDP-D-glucose.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Adler, L.N., Gomez, T.A., Clarke, S.G. and Linster, C.L. A novel GDP-D-glucose phosphorylase involved in quality control of the nucleoside diphosphate sugar pool in Caenorhabditis elegans and mammals. J. Biol. Chem. 286 (2011) 21511-21523. [PMID: 21507950]

EC 2.7.7.79

Accepted name: tRNA^His guanylyltransferase

Reaction: p-tRNA^His + ATP + GTP + H₂O = pGp-tRNA^His + AMP + 2 diphosphate (overall reaction)
(1a) p-tRNA^His + ATP = App-tRNA^His + diphosphate
(1b) App-tRNA^His + GTP = pppGp-tRNA^His + AMP
(1c) pppGp-tRNA^His + H₂O = pGp-tRNA^His + diphosphate

Glossary: p-tRNA^His = 5'-phospho-ribonucleotide-[tRNA^His]
pGp-tRNA^His = 5'-phospho-guanosine-ribonucleotide-[tRNA^His]
App-tRNA^His = 5'-(5'-diphosphoadenosine)-ribonucleotide-[tRNA^His]
pppGp-tRNA^His = 5'-triphospho-ribonucleotide-[tRNA^His]

Other name(s): histidine tRNA guanylyltransferase; Thg1p (ambiguous); Thg1 (ambiguous)

Systematic name: p-tRNA^His:GTP guanylyltransferase (ATP-hydrolysing)

Comments: In eukarya an additional guanosine residue is added post-transcriptionally to the 5'-end of tRNA^His molecules. The addition occurs opposite a universally conserved adenosine⁷³ and is thus the result of a non-templated 3'-5' addition reaction. The additional guanosine residue is an important determinant for aminoacylation by EC 6.1.1.21, histidine—tRNA ligase. The enzyme requires a divalent cation for activity [2]. ATP activation is not required when the substrate contains a 5'-triphosphate (ppp-tRNA^His) [3].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Jahn, D. and Pande, S. Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism. J. Biol. Chem. 266 (1991) 22832-22836. [PMID: 1660462]

2. Pande, S., Jahn, D. and Soll, D. Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties. J. Biol. Chem. 266 (1991) 22826-22831. [PMID: 1660461]

3. Gu, W., Jackman, J.E., Lohan, A.J., Gray, M.W. and Phizicky, E.M. tRNA^His maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNA^His. Genes Dev. 17 (2003) 2889-2901. [PMID: 14633974]

4. Placido, A., Sieber, F., Gobert, A., Gallerani, R., Giege, P. and Marechal-Drouard, L. Plant mitochondria use two pathways for the biogenesis of tRNA^His. Nucleic Acids Res. 38 (2010) 7711-7717. [PMID: 20660484]

5. Jackman, J.E. and Phizicky, E.M. Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase. Biochemistry 47 (2008) 4817-4825. [PMID: 18366186]

6. Hyde, S.J., Eckenroth, B.E., Smith, B.A., Eberley, W.A., Heintz, N.H., Jackman, J.E. and Doublie, S. tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases. Proc. Natl. Acad. Sci. USA 107 (2010) 20305-20310. [PMID: 21059936]

EC 2.7.7.80

Accepted name: molybdopterin-synthase adenylyltransferase

Reaction: ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP

For diagram of reaction click here.

Glossary: small subunit of the molybdopterin synthase = molybdopterin-synthase sulfur-carrier protein = MoaD

Other name(s): MoeB; adenylyltransferase and sulfurtransferase MOCS3

Systematic name: ATP:molybdopterin-synthase adenylyltransferase

Comments: Adenylates the C-terminus of the small subunit of the molybdopterin synthase. This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit. The reaction occurs in prokaryotes and eukaryotes. In the human, the reaction is catalysed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Leimkuhler, S., Wuebbens, M.M. and Rajagopalan, K.V. Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. J. Biol. Chem. 276 (2001) 34695-34701. [PMID: 11463785]

2. Matthies, A., Nimtz, M. and Leimkuhler, S. Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry. Biochemistry 44 (2005) 7912-7920. [PMID: 15910006]

EC 2.7.7.81

Accepted name: pseudaminic acid cytidylyltransferase

Reaction: CTP + 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid = diphosphate + CMP-5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-2-nonulopyranosonic acid

Glossary: CTP:5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-nonulosonic acid cytidylyltransferase

Other name(s): PseF

Systematic name: CTP:5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-α-L-manno-nonulosonic acid cytidylyltransferase

Comments: Mg²⁺ is required for activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Schoenhofen, I.C., McNally, D.J., Brisson, J.R. and Logan, S.M. Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction. Glycobiology 16 (2006) 8C. [PMID: 16751642]

EC 2.7.7.82

Accepted name: CMP-N,N'-diacetyllegionaminic acid synthase

Reaction: CTP + N,N'-diacetyllegionaminate = CMP-N,N'-diacetyllegionaminate + diphosphate

For diagram of reaction click here.

Glossary: legionaminate = 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonate

Other name(s): CMP-N,N'-diacetyllegionaminic acid synthetase; neuA (gene name); legF (gene name)

Systematic name: CTP:N,N'-diacetyllegionaminate cytidylyltransferase

Comments: Isolated from the bacteria Legionella pneumophila and Campylobacter jejuni. Involved in biosynthesis of legionaminic acid, a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates which may include lipopolysaccharide (LPS), capsular polysaccharide, pili and flagella.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Glaze, P.A., Watson, D.C., Young, N.M. and Tanner, M.E. Biosynthesis of CMP-N,N'-diacetyllegionaminic acid from UDP-N,N'-diacetylbacillosamine in Legionella pneumophila. Biochemistry 47 (2008) 3272-3282. [PMID: 18275154]

2. Schoenhofen, I.C., Vinogradov, E., Whitfield, D.M., Brisson, J.R. and Logan, S.M. The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors. Glycobiology 19 (2009) 715-725. [PMID: 19282391]

EC 2.7.7.83

Accepted name: UDP-N-acetylgalactosamine diphosphorylase

Reaction: UTP + N-acetyl-α-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-α-D-galactosamine

Systematic name: UTP:N-acetyl-α-D-galactosamine-1-phosphate uridylyltransferase

Comments: The enzyme from plants and animals also has activity toward N-acetyl-α-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) [1,2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Wang-Gillam, A., Pastuszak, I. and Elbein, A.D. A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J. Biol. Chem. 273 (1998) 27055-27057. [PMID: 9765219]

2. Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F. and Bourne, Y. Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 20 (2001) 6191-6202. [PMID: 11707391]

EC 2.7.7.84

Accepted name: 2'-5' oligoadenylate synthase

Reaction: 3 ATP = pppA2'p5’A2'p5’A + 2 diphosphate

Glossary: pppA2'p5’A2'p5’A = 5'-triphosphoadenylyl-(2'→5')-adenylyl-(2'→5')-adenosine

Other name(s): OAS

Systematic name: ATP:ATP adenylyltransferase (2'-5' linkages-forming)

Comments: The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Kerr, I.M. and Brown, R.E. pppA2'p5’A2'p5’A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells. Proc. Natl. Acad. Sci. USA 75 (1978) 256-260. [PMID: 272640]

2. Martin, E.M., Birdsall, N.J., Brown, R.E. and Kerr, I.M. Enzymic synthesis, characterisation and nuclear-magnetic-resonance spectra of pppA2'p5’A2'p5’A and related oligonucleotides: comparison with chemically synthesised material. Eur. J. Biochem. 95 (1979) 295-307. [PMID: 456356]

3. Hartmann, R., Justesen, J., Sarkar, S.N., Sen, G.C. and Yee, V.C. Crystal structure of the 2'-specific and double-stranded RNA-activated interferon-induced antiviral protein 2'-5'-oligoadenylate synthetase. Mol. Cell 12 (2003) 1173-1185. [PMID: 14636576]

4. Hovanessian, A.G. and Justesen, J. The human 2'-5'oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2'-5' instead of 3'-5' phosphodiester bond formation. Biochimie 89 (2007) 779-788. [PMID: 17408844]

EC 2.7.7.85

Accepted name: diadenylate cyclase

Reaction: 2 ATP = 2 diphosphate + cyclic di-3',5'-adenylate

For diagram of reaction click here.

Glossary: cyclic di-3',5'-adenylate = c-di-AMP = c-di-adenylate = cyclic-bis(3'→5') dimeric AMP

Other name(s): cyclic-di-AMP synthase; dacA (gene name); disA (gene name)

Systematic name: ATP:ATP adenylyltransferase (cyclizing)

Comments: Cyclic di-3',5'-adenylate is a bioactive molecule produced by some bacteria and archaea, which may function as a secondary signalling molecule [1]. The intracellular bacterial pathogen Listeria monocytogenes secretes it into the host’s cytosol, where it triggers a cytosolic pathway of innate immunity [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Witte, G., Hartung, S., Buttner, K. and Hopfner, K.P. Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates. Mol. Cell 30 (2008) 167-178. [PMID: 18439896]

2. Woodward, J.J., Iavarone, A.T. and Portnoy, D.A. c-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response. Science 328 (2010) 1703-1705. [PMID: 20508090]

EC 2.7.7.86

Accepted name: cyclic GMP-AMP synthase

Reaction: ATP + GTP = 2 diphosphate + cyclic Gp(2'-5')Ap(3'-5') (overall reaction)
(1a) ATP + GTP = pppGp(2'-5')A + diphosphate
(1b) pppGp(2'-5')A = cyclic Gp(2'-5')Ap(3'-5') + diphosphate

Glossary: cyclic Gp(2'-5')Ap(3'-5') = cyclo[(3'→5')-guanylyl-(2'→5')-adenylyl]

Other name(s): cGAMP synthase; cGAS

Systematic name: ATP:GTP adenylyltransferase (cyclizing)

Comments: Cyclic Gp(2'-5')Ap(3'-5') is a signalling molecule in mammalian cells that triggers the production of type I interferons and other cytokines.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:

References:

1. Sun, L., Wu, J., Du, F., Chen, X. and Chen, Z.J. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 339 (2013) 786-791. [PMID: 23258413]

2. Ablasser, A., Goldeck, M., Cavlar, T., Deimling, T., Witte, G., Rohl, I., Hopfner, K.P., Ludwig, J. and Hornung, V. cGAS produces a 2'-5'-linked cyclic dinucleotide second messenger that activates STING. Nature 498 (2013) 380-384. [PMID: 23722158]

EC 2.7.7.87

Accepted name: L-threonylcarbamoyladenylate synthase

Reaction: L-threonine + ATP + HCO₃^- = L-threonylcarbamoyladenylate + diphosphate + H₂O

For diagram of reaction click here.

Other name(s): yrdC (gene name); Sua5; ywlC (gene name)

Systematic name: ATP:L-threonyl,HCO₃^- adenylyltransferase

Comments: The enzyme is involved in the synthesis of N⁶-threonylcarbamoyladenosine³⁷ in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNA^Ile, tRNA^Thr, tRNA^Asn, tRNA^Lys, tRNA^Ser and tRNA^Arg [6].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. El Yacoubi, B., Lyons, B., Cruz, Y., Reddy, R., Nordin, B., Agnelli, F., Williamson, J.R., Schimmel, P., Swairjo, M.A. and de Crecy-Lagard, V. The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA. Nucleic Acids Res. 37 (2009) 2894-2909. [PMID: 19287007]

2. Harris, K.A., Jones, V., Bilbille, Y., Swairjo, M.A. and Agris, P.F. YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase. RNA 17 (2011) 1678-1687. [PMID: 21775474]

3. Kuratani, M., Kasai, T., Akasaka, R., Higashijima, K., Terada, T., Kigawa, T., Shinkai, A., Bessho, Y. and Yokoyama, S. Crystal structure of Sulfolobus tokodaii Sua5 complexed with L-threonine and AMPPNP. Proteins 79 (2011) 2065-2075. [PMID: 21538543]

4. Lauhon, C.T. Mechanism of N⁶-threonylcarbamoyladenonsine (t⁶A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP. Biochemistry 51 (2012) 8950-8963. [PMID: 23072323]

5. Deutsch, C., El Yacoubi, B., de Crecy-Lagard, V. and Iwata-Reuyl, D. Biosynthesis of threonylcarbamoyl adenosine (t⁶A), a universal tRNA nucleoside. J. Biol. Chem. 287 (2012) 13666-13673. [PMID: 22378793]

6. Perrochia, L., Crozat, E., Hecker, A., Zhang, W., Bareille, J., Collinet, B., van Tilbeurgh, H., Forterre, P. and Basta, T. In vitro biosynthesis of a universal t⁶A tRNA modification in Archaea and Eukarya. Nucleic Acids Res. 41 (2013) 1953-1964. [PMID: 23258706]

7. Wan, L.C.K., Mao, D.Y.L., Neculai, D., Strecker, J., Chiovitti, D., Kurinov, I., Poda, G., Thevakumaran, N., Yuan, F., Szilard, R.K., Lissina, E., Nislow, C., Caudy, A.A., Durocher, D. and Sicheri, F. Reconstitution and characterization of eukaryotic N⁶-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Res. (2013) . [PMID: 23620299]

EC 2.7.7.88

Accepted name: GDP polyribonucleotidyltransferase

Reaction: (5')pppAACA-[mRNA] + GDP = diphosphate + G(5')pppAACA-[mRNA] (overall reaction)
(1a) (5')pppAACA-[mRNA] + [protein L]-L-histidine = diphosphate + [protein L]-L-histidyl-(5')phosphonato-AACA-[mRNA] + H₂O
(1b) [protein L]-L-histidyl-(5')phosphonato-AACA-[mRNA] + GDP + H₂O = [protein L]-L-histidine + G(5')pppAACA-[mRNA]

Other name(s): PRNTase; 5'-triphospho-mRNA:GDP 5'-phosphopolyribonucleotidyltransferase [G(5')ppp-mRNA-forming]

Systematic name: (5')pppAACA-[mRNA]:GDP 5'-phosphopolyribonucleotidyltransferase [(5')pppAACA-[mRNA]-forming]

Comments: The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses and lyssaviruses) is specific for mRNAs with sequences starting with AACA. cf. EC 2.7.7.50, mRNA guanylyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:

References:

1. Ogino, T. and Banerjee, A.K. Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus. Mol. Cell 25 (2007) 85-97. [PMID: 17218273]

2. Ogino, T. and Banerjee, A.K. Formation of guanosine(5')tetraphospho(5')adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus. J. Virol. 82 (2008) 7729-7734. [PMID: 18495767]

3. Ogino, T., Yadav, S.P. and Banerjee, A.K. Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase. Proc. Natl. Acad. Sci. USA 107 (2010) 3463-3468. [PMID: 20142503]

4. Ogino, T. and Banerjee, A.K. The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity. J. Gen. Virol. 91 (2010) 1311-1314. [PMID: 20107017]

5. Ogino, T. and Banerjee, A.K. An unconventional pathway of mRNA cap formation by vesiculoviruses. Virus Res. 162 (2011) 100-109. [PMID: 21945214]

6. Ogino, M., Ito, N., Sugiyama, M. and Ogino, T. The rabies virus L protein catalyzes mRNA capping with GDP polyribonucleotidyltransferase activity. Viruses 8 (2016) 144. [PMID: 27213429]

EC 2.7.7.89

Accepted name: [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase

Reaction: [glutamine synthetase]-O⁴-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP

Other name(s): adenylyl-[glutamine—synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O⁴-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate—ammonia ligase]-adenylyl-L-tyrosine phosphorylase

Systematic name: [glutamine synthetase]-O⁴-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase

Comments: This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase) [3,5]. The two activities are present on separate domains.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:

References:

1. Anderson, W.B. and Stadtman, E.R. Glutamine synthetase deadenylation: a phosphorolytic reaction yielding ADP as nucleotide product. Biochem. Biophys. Res. Commun. 41 (1970) 704-709. [PMID: 4920873]

2. Anderson, W.B. and Stadtman, E.R. Purification and functional roles of the P I and P II components of Escherichia coli glutamine synthetase deadenylylation system. Arch. Biochem. Biophys. 143 (1971) 428-443. [PMID: 4934180]

3. Jaggi, R., van Heeswijk, W.C., Westerhoff, H.V., Ollis, D.L. and Vasudevan, S.G. The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J. 16 (1997) 5562-5571. [PMID: 9312015]

4. Xu, Y., Wen, D., Clancy, P., Carr, P.D., Ollis, D.L. and Vasudevan, S.G. Expression, purification, crystallization, and preliminary X-ray analysis of the N-terminal domain of Escherichia coli adenylyl transferase. Protein Expr. Purif. 34 (2004) 142-146. [PMID: 14766310]

5. Xu, Y., Zhang, R., Joachimiak, A., Carr, P.D., Huber, T., Vasudevan, S.G. and Ollis, D.L. Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. Structure 12 (2004) 861-869. [PMID: 15130478]

EC 2.7.7.90

Accepted name: CMP-8-amino-3,8-dideoxy-manno-octulosonate cytidylyltransferase

Reaction: CTP + 8-amino-3,8-dideoxy-α-D-manno-octulosonate = diphosphate + CMP-8-amino-3,8-dideoxy-α-D-manno-octulosonate

Other name(s): kdsB (gene name, ambiguous)

Systematic name: CTP:8-amino-3,8-dideoxy-α-D-manno-octulosonate cytidylyltransferase

Comments: The enzyme, characterized from the bacterium Shewanella oneidensis MR-1, acts on the 8-aminated from of 3-deoxy-α-D-manno-octulosonate (Kdo). cf. EC 2.7.7.38, 3-deoxy-manno-octulosonate cytidylyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Gattis, S.G., Chung, H.S., Trent, M.S. and Raetz, C.R. The origin of 8-amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N) in the lipopolysaccharide of Shewanella oneidensis, J. Biol. Chem. 288 (2013) 9216-9225. [PMID: 23413030]

EC 2.7.7.91

Accepted name: valienol-1-phosphate guanylyltransferase

Reaction: GTP + valienol 1-phosphate = diphosphate + GDP-valienol

Glossary: valienol 1-phosphate = (1S,4R,5S,6R)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl phosphate

Other name(s): vldB (gene name)

Systematic name: GTP:valienol 1-phosphate guanylyltransferase

Comments: The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, is involved in the biosynthesis of the antifungal agent validamycin A.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Yang, J., Xu, H., Zhang, Y., Bai, L., Deng, Z. and Mahmud, T. Nucleotidylation of unsaturated carbasugar in validamycin biosynthesis. Org. Biomol. Chem. 9 (2011) 438-449. [PMID: 20981366]

2. Asamizu, S., Yang, J., Almabruk, K.H. and Mahmud, T. Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in validamycin a biosynthesis. J. Am. Chem. Soc. 133 (2011) 12124-12135. [PMID: 21766819]

EC 2.7.7.92

Accepted name: 3-deoxy-D-glycero-D-galacto-nononate cytidylyltransferase

Reaction: CTP + 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate = diphosphate + CMP-3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate

Systematic name: CTP:3-deoxy-D-glycero-D-galacto-nononate cytidylyltransferase

Comments: The enzyme is part of the biosynthesis pathway of the sialic acid 3-deoxy-D-glycero-D-galacto-nononate (Kdn). Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Terada, T., Kitazume, S., Kitajima, K., Inoue, S., Ito, F., Troy, F.A. and Inoue, Y. Synthesis of CMP-deaminoneuraminic acid (CMP-KDN) using the CTP:CMP-3-deoxynonulosonate cytidylyltransferase from rainbow trout testis. Identification and characterization of a CMP-KDN synthetase. J. Biol. Chem. 268 (1993) 2640-2648. [PMID: 8381411]

2. Terada, T., Kitajima, K., Inoue, S., Koppert, K., Brossmer, R. and Inoue, Y. Substrate specificity of rainbow trout testis CMP-3-deoxy-D-glycero-D-galacto-nonulosonic acid (CMP-Kdn) synthetase: kinetic studies of the reaction of natural and synthetic analogues of nonulosonic acid catalyzed by CMP-Kdn synthetase. Eur. J. Biochem. 236 (1996) 852-855. [PMID: 8665905]

3. Nakata, D., Munster, A.K., Gerardy-Schahn, R., Aoki, N., Matsuda, T. and Kitajima, K. Molecular cloning of a unique CMP-sialic acid synthetase that effectively utilizes both deaminoneuraminic acid (KDN) and N-acetylneuraminic acid (Neu5Ac) as substrates. Glycobiology 11 (2001) 685-692. [PMID: 11479279]

4. Tiralongo, J., Fujita, A., Sato, C., Kitajima, K., Lehmann, F., Oschlies, M., Gerardy-Schahn, R. and Munster-Kuhnel, A.K. The rainbow trout CMP-sialic acid synthetase utilises a nuclear localization signal different from that identified in the mouse enzyme. Glycobiology 17 (2007) 945-954. [PMID: 17580313]

5. Wang, L., Lu, Z., Allen, K.N., Mariano, P.S. and Dunaway-Mariano, D. Human symbiont Bacteroides thetaiotaomicron synthesizes 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). Chem. Biol. 15 (2008) 893-897. [PMID: 18804026]

EC 2.7.7.93

Accepted name: phosphonoformate cytidylyltransferase

Reaction: CTP + phosphonoformate = CMP-5'-phosphonoformate + diphosphate

Other name(s): phpF (gene name)

Systematic name: CTP:phosphonoformate cytidylyltransferase

Comments: The enzyme, characterized from the bacterium Streptomyces viridochromogenes, participates in the biosynthesis of the herbicide antibiotic bialaphos. The enzyme from the bacterium Kitasatospora phosalacinea participates in the biosynthesis of the related compound phosalacine. Both compounds contain the nonproteinogenic amino acid L-phosphinothricin that acts as a potent inhibitor of EC 6.3.1.2, glutamine synthetase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Blodgett, J.A., Thomas, P.M., Li, G., Velasquez, J.E., van der Donk, W.A., Kelleher, N.L. and Metcalf, W.W. Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide. Nat. Chem. Biol. 3 (2007) 480-485. [PMID: 17632514]

[EC 2.7.7.94 Transferred entry: 4-hydroxyphenylalkanoate adenylyltransferase. Now EC 6.2.1.51, 4-hydroxyphenylalkanoate adenylyltransferase FadD29 (EC 2.7.7.94 created 2016, deleted 2017)]

[EC 2.7.7.95 Transferred entry: mycocerosic acid adenylyltransferase. Now EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28 (EC 2.7.7.95 created 2016, deleted 2017)]

EC 2.7.7.96

Accepted name: ADP-D-ribose pyrophosphorylase

Reaction: ATP + D-ribose 5-phosphate = diphosphate + ADP-D-ribose

Other name(s): NUDIX5; NUDT5 (gene name); diphosphate—ADP-D-ribose adenylyltransferase; diphosphate adenylyltransferase (ambiguous)

Systematic name: ATP:D-ribose 5-phosphate adenylyltransferase

Comments: The human enzyme produces ATP in nuclei in situations of high energy demand, such as chromatin remodeling. The reaction is dependent on the presence of diphosphate. In its absence the enzyme catalyses the reaction of EC 3.6.1.13, ADP-ribose diphosphatase. cf. EC 2.7.7.35, ADP ribose phosphorylase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Wright, R.H., Lioutas, A., Le Dily, F., Soronellas, D., Pohl, A., Bonet, J., Nacht, A.S., Samino, S., Font-Mateu, J., Vicent, G.P., Wierer, M., Trabado, M.A., Schelhorn, C., Carolis, C., Macias, M.J., Yanes, O., Oliva, B. and Beato, M. ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling. Science 352 (2016) 1221-1225. [PMID: 27257257]

EC 2.7.7.97

Accepted name: 3-hydroxy-4-methylanthranilate adenylyltransferase

Reaction: ATP + 3-hydroxy-4-methylanthranilate = diphosphate + 3-hydroxy-4-methylanthranilyl-adenylate

Other name(s): acmA (gene name); sibE (gene name); actinomycin synthase I; 4-MHA-activating enzyme; ACMS I; actinomycin synthetase I; 4-MHA pentapeptide lactone synthase AcmA

Systematic name: ATP:3-hydroxy-4-methylanthranilate adenylyltransferase

Comments: The enzyme, characterized from the bacteria Streptomyces anulatus and Streptosporangium sibiricum, activates 3-hydroxy-4-methylanthranilate, a precursor of actinomycin antibiotics and the antitumor antibiotic sibiromycin, to an adenylate form, so it can be loaded onto a dedicated aryl-carrier protein.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Pfennig, F., Schauwecker, F. and Keller, U. Molecular characterization of the genes of actinomycin synthetase I and of a 4-methyl-3-hydroxyanthranilic acid carrier protein involved in the assembly of the acylpeptide chain of actinomycin in Streptomyces. J. Biol. Chem. 274 (1999) 12508-12516. [PMID: 10212227]

2. Giessen, T.W., Kraas, F.I. and Marahiel, M.A. A four-enzyme pathway for 3,5-dihydroxy-4-methylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin. Biochemistry 50 (2011) 5680-5692. [PMID: 21612226]

[EC 2.7.7.98 Transferred entry: 4-hydroxybenzoate adenylyltransferase. Now EC 6.2.1.50, 4-hydroxybenzoate adenylyltransferase FadD22 (EC 2.7.7.98 created 2017, deleted 2017)]

EC 2.7.7.99

Accepted name: N-acetyl-α-D-muramate 1-phosphate uridylyltransferase

Reaction: UDP + N-acetyl-α-D-muramate 1-phosphate = UDP-N-acetyl-α-D-muramate + phosphate

Glossary: N-acetyl-D-muramate = 3-O-[(1R)-1-carboxyethyl]-2-acetoxy-2-deoxy-D-glucopyranose

Other name(s): murU (gene name)

Systematic name: UDP:N-acetyl-α-D-muramate 1-phosphate uridylyltransferase

Comments: The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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]

2. Renner-Schneck, M., Hinderberger, I., Gisin, J., Exner, T., Mayer, C. and Stehle, T. Crystal structure of the N-acetylmuramic acid α-1-phosphate (MurNAc-α1-P) uridylyltransferase MurU, a minimal sugar nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens. J. Biol. Chem. 290 (2015) 10804-10813. [PMID: 25767118]

EC 2.7.7.100

Accepted name: SAMP-activating enzyme

Reaction: ATP + [SAMP]-Gly-Gly = diphosphate + [SAMP]-Gly-Gly-AMP

Glossary: SAMP = small archaeal modifier protein = ubiquitin-like small archaeal modifier protein

Other name(s): UbaA (ambiguous); SAMP-activating enzyme E1 (ambiguous)

Systematic name: ATP:SAMP adenylyltransferase

Comments: Contains Zn²⁺. The enzyme catalyses the activation of SAMPs (Small Archaeal Modifier Proteins), which are ubiquitin-like proteins found only in the Archaea, by catalysing the ATP-dependent formation of a SAMP adenylate in which the C-terminal glycine of SAMP is bound to AMP via an acyl-phosphate linkage. The product of this activity can accept a sulfur atom to form a thiocarboxylate moiety that acts as a sulfur carrier involved in thiolation of tRNA and other metabolites such as molybdopterin. Alternatively, the enzyme can also catalyse the transfer of SAMP from its activated form to an internal cysteine residue, leading to a process termed SAMPylation (see EC 6.2.1.55, E1 SAMP-activating enzyme).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Miranda, H.V., Nembhard, N., Su, D., Hepowit, N., Krause, D.J., Pritz, J.R., Phillips, C., Soll, D. and Maupin-Furlow, J.A. E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea. Proc. Natl Acad. Sci. USA 108 (2011) 4417-4422. [PMID: 21368171]

2. Maupin-Furlow, J.A. Ubiquitin-like proteins and their roles in archaea. Trends Microbiol 21 (2013) 31-38. [PMID: 23140889]

3. Hepowit, N.L., de Vera, I.M., Cao, S., Fu, X., Wu, Y., Uthandi, S., Chavarria, N.E., Englert, M., Su, D., Sll, D., Kojetin, D.J. and Maupin-Furlow, J.A. Mechanistic insight into protein modification and sulfur mobilization activities of noncanonical E1 and associated ubiquitin-like proteins of Archaea. FEBS J. 283 (2016) 3567-3586. [PMID: 27459543]

EC 2.7.7.101

Accepted name: DNA primase DnaG

Reaction: ssDNA + n NTP = ssDNA/pppN(pN)_n-1 hybrid + (n-1) diphosphate

Other name(s): DnaG

Systematic name: nucleotide 5'-triphosphate:single-stranded DNA nucleotidyltransferase (DNA-RNA hybrid synthesizing)

Comments: The enzyme catalyses the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase. It is found in bacteria and archaea. The latter also have a second primase system (EC 2.7.7.102, DNA primase AEP).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Rowen, L. and Kornberg, A. Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains. J. Biol. Chem. 253 (1978) 758-764. [PMID: 340457]

2. Ilyina, T.V., Gorbalenya, A.E. and Koonin, E.V. Organization and evolution of bacterial and bacteriophage primase-helicase systems. J. Mol. Evol. 34 (1992) 351-357. [PMID: 1569588]

3. Frick, D.N. and Richardson, C.C. DNA primases. Annu. Rev. Biochem. 70 (2001) 39-80. [PMID: 11395402]

4. Zuo, Z., Rodgers, C.J., Mikheikin, A.L. and Trakselis, M.A. Characterization of a functional DnaG-type primase in archaea: implications for a dual-primase system. J. Mol. Biol. 397 (2010) 664-676. [PMID: 20122937]

EC 2.7.7.102

Accepted name: DNA primase AEP

Reaction: (1) ssDNA + n NTP = ssDNA/pppN(pN)_n-1 hybrid + (n-1) diphosphate
(2) ssDNA + n dNTP = ssDNA/pppdN(pdN)_n-1 hybrid + (n-1) diphosphate

Other name(s): archaeo-eukaryotic primase; AEP; PrimPol

Systematic name: (deoxy)nucleotide 5'-triphosphate:single-stranded DNA (deoxy)nucleotidyltransferase (DNA or DNA-RNA hybrid synthesizing)

Comments: The enzyme, which is found in eukaryota and archaea, catalyses the synthesis of short RNA or DNA sequences which are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Desogus, G., Onesti, S., Brick, P., Rossi, M. and Pisani, F.M. Identification and characterization of a DNA primase from the hyperthermophilic archaeon Methanococcus jannaschii. Nucleic Acids Res. 27 (1999) 4444-4450. [PMID: 10536154]

2. Arezi, B. and Kuchta, R.D. Eukaryotic DNA primase. Trends Biochem. Sci. 25 (2000) 572-576. [PMID: 11084371]

3. Liu, L., Komori, K., Ishino, S., Bocquier, A.A., Cann, I.K., Kohda, D. and Ishino, Y. The archaeal DNA primase: biochemical characterization of the p41-p46 complex from Pyrococcus furiosus. J. Biol. Chem 276 (2001) 45484-45490. [PMID: 11584001]

4. Lao-Sirieix, S.H. and Bell, S.D. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal nucleotidyl transferase activities. J. Mol. Biol. 344 (2004) 1251-1263. [PMID: 15561142]

5. Baranovskiy, A.G., Zhang, Y., Suwa, Y., Babayeva, N.D., Gu, J., Pavlov, Y.I. and Tahirov, T.H. Crystal structure of the human primase. J. Biol. Chem 290 (2015) 5635-5646. [PMID: 25550159]

6. Guilliam, T.A., Keen, B.A., Brissett, N.C. and Doherty, A.J. Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes. Nucleic Acids Res. 43 (2015) 6651-6664. [PMID: 26109351]

EC 2.7.7.103

Accepted name: L-glutamine-phosphate cytidylyltransferase

Reaction: CTP + N⁵-phospho-L-glutamine = diphosphate + N⁵-(cytidine 5'-diphosphoramidyl)-L-glutamine

Systematic name: CTP:phosphoglutamine cytidylyltransferase

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., Brown, H.A., Holden, H.M. and Raushel, F.M. Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni. Biochemistry 56 (2017) 6079-6082. [PMID: 29023101]

EC 2.7.7.104

Accepted name: 2-hydroxyethylphosphonate cytidylyltransferase

Reaction: 2-hydroxyethylphosphonate + CTP = cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + diphosphate

Other name(s): Fom1

Systematic name: CTP:2-hydroxyethylphosphonate cytidylyltransferase

Comments: The enzyme, isolated from the bacterium Streptomyces wedmorensis, is involved in fosfomycin biosynthesis. The enzyme also is active as EC 5.4.2.9 phosphoenolpyruvate mutase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:

References:

1. Cho, S.H., Kim, S.Y., Tomita, T., Shiraishi, T., Park, J.S., Sato, S., Kudo, F., Eguchi, T., Funa, N., Nishiyama, M. and Kuzuyama, T. Fosfomycin biosynthesis via transient cytidylylation of 2-hydroxyethylphosphonate by the bifunctional Fom1 enzyme. ACS Chem. Biol. 12 (2017) 2209-2215. [PMID: 28727444]

EC 2.7.7.105

Accepted name: phosphoenolpyruvate guanylyltransferase

Reaction: phosphoenolpyruvate + GTP = enolpyruvoyl-2-diphospho-5'-guanosine + diphosphate

Other name(s): fbiD (gene name)

Systematic name: GTP:phosphoenolpyruvate guanylyltransferase

Comments: This enzyme is involved in the biosynthesis of coenzyme F₄₂₀, a redox-active cofactor, in mycobacteria. cf. EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase and EC 2.7.7.106, 3-phospho-(R)-glycerate guanylyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc PDB, CAS registry number:

References:

1. Bashiri, G., Antoney, J., Jirgis, E.NM., Shah, M.V., Ney, B., Copp, J., Stuteley, S.M., Sreebhavan, S., Palmer, B., Middleditch, M., Tokuriki, N., Greening, C., Scott, C., Baker, E.N. and Jackson, C.J. A revised biosynthetic pathway for the cofactor F₄₂₀ in prokaryotes. Nat. Commun. 10 (2019) 1558. [PMID: 30952857]

2. Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088-2094. [PMID: 31469543]

EC 2.7.7.106

Accepted name: 3-phospho-D-glycerate guanylyltransferase

Reaction: 3-phospho-D-glycerate + GTP = 3-(D-glyceryl)-diphospho-5'-guanosine + diphosphate

Other name(s): cofC (gene name) (ambiguous)

Systematic name: GTP:3-phospho-D-glycerate guanylyltransferase

Comments: The enzyme, characterized from the Gram-negative bacterium Paraburkholderia rhizoxinica, participates in the biosynthesis of 3PG-factor 420. The enzyme can also accept 2-phospho-L-lactate and phosphoenolpyruvate, but activity is much higher with 3-phospho-D-glycerate. cf. EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase and EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc PDB, CAS registry number:

References:

1. Braga, D., Last, D., Hasan, M., Guo, H., Leichnitz, D., Uzum, Z., Richter, I., Schalk, F., Beemelmanns, C., Hertweck, C. and Lackner, G. Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F₄₂₀. ACS Chem. Biol. 14 (2019) 2088-2094. [PMID: 31469543]

EC 2.7.7.107

Accepted name: (2-aminoethyl)phosphonate cytidylyltransferase

Reaction: CTP + (2-aminoethyl)phosphonate = diphosphate + CMP-(2-aminoethyl)phosphonate

Other name(s): pntC (gene name)

Systematic name: CTP:(2-aminoethyl)phosphonate cytidylyltransferase

Comments: This bacterial enzyme activates (2-aminoethyl)phosphonate for incorporation into cell wall phosphonoglycans and phosphonolipids, much like EC 2.7.7.15, choline-phosphate cytidylyltransferase, activates phosphocholine for the same purpose.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Rice, K., Batul, K., Whiteside, J., Kelso, J., Papinski, M., Schmidt, E., Pratasouskaya, A., Wang, D., Sullivan, R., Bartlett, C., Weadge, J.T., Van der Kamp, M.W., Moreno-Hagelsieb, G., Suits, M.D. and Horsman, G.P. The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis. Nat. Commun. 10 (2019) 3698. [PMID: 31420548]

EC 2.7.7.108

Accepted name: protein adenylyltransferase

Reaction: (1) ATP + a [protein]-L-serine = diphosphate + a [protein]-O-(5'-adenylyl)-L-serine
(1) ATP + a [protein]-L-threonine = diphosphate + a [protein]-O-(5'-adenylyl)-L-threonine
(1) ATP + a [protein]-L-tyrosine = diphosphate + a [protein]-O-(5'-adenylyl)-L-tyrosine

Other name(s): AMPylase; selO (gene name); FMP40 (gene name); SELENOO (gene name); IbpA; VopS; DrrA; FICD (gene name)

Systematic name: [protein] L-serine/L-threonine/L-tyrosine adenylyltransferase

Comments: The enzyme, commonly referred to as AMPylase, transfers an adenylyl (adenosine 5'-phosphate) group from ATP to L-serine, L-threonine, and L-tyrosine residues in its target protein substrates. AMPylation is found in both prokaryotes and eukaryotes. In bacteria AMPylases are abundant enzymes that either regulate the function of endogenous bacterial proteins or are translocated into host cells to hijack host cell signalling processes. Metazoans AMPylases are either enzymes containing a conserved Fic domain that primarily modify the ER-resident chaperone BiP, or mitochondrial selenocysteine-containing proteins (SelO) involved in redox signalling.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Xiao, J., Worby, C.A., Mattoo, S., Sankaran, B. and Dixon, J.E. Structural basis of Fic-mediated adenylylation. Nat. Struct. Mol. Biol. 17 (2010) 1004-1010. [PMID: 20622875]

2. Palanivelu, D.V., Goepfert, A., Meury, M., Guye, P., Dehio, C. and Schirmer, T. Fic domain-catalyzed adenylylation: insight provided by the structural analysis of the type IV secretion system effector BepA. Protein Sci. 20 (2011) 492-499. [PMID: 21213248]

3. Truttmann, M.C., Cruz, V.E., Guo, X., Engert, C., Schwartz, T.U. and Ploegh, H.L. The Caenorhabditis elegans protein FIC-1 is an AMPylase that covalently modifies heat-shock 70 family proteins, translation elongation factors and histones. PLoS Genet. 12 (2016) e1006023. [PMID: 27138431]

4. Sreelatha, A., Yee, S.S., Lopez, V.A., Park, B.C., Kinch, L.N., Pilch, S., Servage, K.A., Zhang, J., Jiou, J., Karasiewicz-Urbanska, M., Lobocka, M., Grishin, N.V., Orth, K., Kucharczyk, R., Pawlowski, K., Tomchick, D.R. and Tagliabracci, V.S. Protein AMPylation by an evolutionarily conserved pseudokinase. Cell 175 (2018) 809-821. [PMID: 30270044]

5. Bardwell, L. Pseudokinases: Flipping the ATP for AMPylation. Curr. Biol. 29 (2019) R23-R25. [PMID: 30620911]

6. Chatterjee, B.K. and Truttmann, M.C. Fic and non-Fic AMPylases: protein AMPylation in metazoans. Open Biol 11 (2021) 210009. [PMID: 33947243]