Enzyme Nomenclature

EC 2.7.1 Phosphotransferases with an Alcohol Group as Acceptor (Continued)

Continued from:
EC 2.7.1.1 to EC 2.7.1.50
EC 2.7.1.51 to EC 2.7.1.100

Contents

EC 2.7.1.151 inositol-polyphosphate multikinase
EC 2.7.1.152 now EC 2.7.4.21
EC 2.7.1.153 phosphatidylinositol-4,5-bisphosphate 3-kinase
EC 2.7.1.154 phosphatidylinositol-4-phosphate 3-kinase
EC 2.7.1.155 diphosphoinositol-pentakisphosphate kinase
EC 2.7.1.155 now EC 2.7.4.24
EC 2.7.1.156 adenosylcobinamide kinase
EC 2.7.1.157 N-acetylgalactosamine kinase
EC 2.7.1.158 inositol-pentakisphosphate 2-kinase
EC 2.7.1.159 inositol-1,3,4-trisphosphate 5/6-kinase
EC 2.7.1.160 2'-phosphotransferase
EC 2.7.1.161 CTP-dependent riboflavin kinase
EC 2.7.1.162 N-acetylhexosamine 1-kinase
EC 2.7.1.163 hygromycin B 4-O-kinase
EC 2.7.1.164 O-phosphoseryl-tRNASec kinase
EC 2.7.1.165 glycerate 2-kinase
EC 2.7.1.166 3-deoxy-D-manno-octulosonic acid kinase
EC 2.7.1.167 D-glycero-β-D-manno-heptose-7-phosphate kinase
EC 2.7.1.168 D-glycero-α-D-manno-heptose-7-phosphate kinase
EC 2.7.1.169 pantoate kinase
EC 2.7.1.170 anhydro-N-acetylmuramic acid kinase
EC 2.7.1.171 protein-fructosamine 3-kinase
EC 2.7.1.172 protein-ribulosamine 3-kinase
EC 2.7.1.173 nicotinate riboside kinase
EC 2.7.1.174 diacylglycerol kinase (CTP)
EC 2.7.1.175 maltokinase
EC 2.7.1.176 UDP-N-acetylglucosamine kinase
EC 2.7.1.177 L-threonine kinase
EC 2.7.1.178 2-dehydro-3-deoxyglucono/galactono-kinase
EC 2.7.1.179 kanosamine kinase
EC 2.7.1.180 FAD:protein FMN transferase
EC 2.7.1.181 polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase
EC 2.7.1.182 phytol kinase
EC 2.7.1.183 glycoprotein-mannosyl O6-kinase
EC 2.7.1.184 sulfofructose kinase
EC 2.7.1.185 mevalonate 3-kinase
EC 2.7.1.186 mevalonate-3-phosphate 5-kinase
EC 2.7.1.187 acarbose 7IV-phosphotransferase
EC 2.7.1.188 2-epi-5-epi-valiolone 7-kinase
EC 2.7.1.189 autoinducer-2 kinase
EC 2.7.1.190 aminoglycoside 2''-phosphotransferase
EC 2.7.1.191 protein-Nπ-phosphohistidine—D-mannose phosphotransferase
EC 2.7.1.192 protein-Nπ-phosphohistidine—N-acetylmuramate phosphotransferase
EC 2.7.1.193 protein-Nπ-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase
EC 2.7.1.194 protein-Nπ-phosphohistidine—L-ascorbate phosphotransferase
EC 2.7.1.195 protein-Nπ-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase
EC 2.7.1.196 protein-Nπ-phosphohistidine—N,N'-diacetylchitobiose phosphotransferase
EC 2.7.1.197 protein-Nπ-phosphohistidine—D-mannitol phosphotransferase
EC 2.7.1.198 protein-Nπ-phosphohistidine—D-sorbitol phosphotransferase
EC 2.7.1.199 protein-Nπ-phosphohistidine—D-glucose phosphotransferase
EC 2.7.1.200 protein-Nπ-phosphohistidine—galactitol phosphotransferase
EC 2.7.1.201 protein-Nπ-phosphohistidine—trehalose phosphotransferase
EC 2.7.1.202 protein-Nπ-phosphohistidine—D-fructose phosphotransferase
EC 2.7.1.203 protein-Nπ-phosphohistidine—D-glucosaminate phosphotransferase
EC 2.7.1.204 protein-Nπ-phosphohistidine—D-galactose phosphotransferase
EC 2.7.1.205 protein-Nπ-phosphohistidine—D-cellobiose phosphotransferase
EC 2.7.1.206 protein-Nπ-phosphohistidine—L-sorbose phosphotransferase
EC 2.7.1.207 protein-Nπ-phosphohistidine—lactose phosphotransferase
EC 2.7.1.208 protein-Nπ-phosphohistidine—maltose phosphotransferase
EC 2.7.1.209 L-erythrulose 1-kinase
EC 2.7.1.210 D-erythrulose 4-kinase
EC 2.7.1.211 protein-Nπ-phosphohistidine—sucrose phosphotransferase
EC 2.7.1.212 α-D-ribose-1-phosphate 5-kinase (ADP)
EC 2.7.1.213 cytidine kinase
EC 2.7.1.214 C7-cyclitol 7-kinase
EC 2.7.1.215 erythritol kinase (D-erythritol 1-phosphate-forming)
EC 2.7.1.216 farnesol kinase
EC 2.7.1.217 3-dehydrotetronate 4-kinase
EC 2.7.1.218 fructoselysine 6-kinase
EC 2.7.1.219 D-threonate 4-kinase
EC 2.7.1.220 D-erythronate 4-kinase
EC 2.7.1.221 N-acetylmuramate 1-kinase
EC 2.7.1.222 4-hydroxytryptamine kinase
EC 2.7.1.223 aminoimidazole riboside kinase
EC 2.7.1.224 cytidine diphosphoramidate kinase
EC 2.7.1.225 L-serine kinase (ATP)
EC 2.7.1.226 L-serine kinase (ADP)

Entries

EC 2.7.1.151

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 2.7.1.151 created 2002, modified 2006]

[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)]

EC 2.7.1.153

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]

[EC 2.7.1.153 created 2002]

EC 2.7.1.154

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 2.7.1.154 created 2002]

[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)]

EC 2.7.1.156

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]

[EC 2.7.1.156 created 2004]

EC 2.7.1.157

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]

[EC 2.7.1.157 created 2005]

EC 2.7.1.158

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]

[EC 2.7.1.158 created 2006]

EC 2.7.1.159

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].

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]

[EC 2.7.1.159 created 2006]

EC 2.7.1.160

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, 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]

[EC 2.7.1.160 created 2006]

EC 2.7.1.161

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]

[EC 2.7.1.161 created 2008]

EC 2.7.1.162

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, 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]

[EC 2.7.1.162 created 2008]

EC 2.7.1.162

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]

[EC 2.7.1.163 created 2009]

EC 2.7.1.164

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]

[EC 2.7.1.164 created 2009]

EC 2.7.1.165

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]

[EC 2.7.1.165 created 2010]

EC 2.7.1.166

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]

[EC 2.7.1.166 created 2010, modified 2011]

EC 2.7.1.167

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, 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]

[EC 2.7.1.167 created 2010]

EC 2.7.1.168

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, 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]

[EC 2.7.1.168 created 2010]

EC 2.7.1.169

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, 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]

[EC 2.7.1.169 created 2011]

EC 2.7.1.170

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]

[EC 2.7.1.170 created 2011, modified 2011]

EC 2.7.1.171

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]

[EC 2.7.1.171 created 2011]

EC 2.7.1.172

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, 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]

[EC 2.7.1.172 created 2011]

EC 2.7.1.173

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]

[EC 2.7.1.173 created 2012]

EC 2.7.1.174

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]

[EC 2.7.1.174 created 2012, modified 2013]

EC 2.7.1.175

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, 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]

[EC 2.7.1.175 created 2012]

EC 2.7.1.176

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]

[EC 2.7.1.176 created 2012]

EC 2.7.1.177

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]

[EC 2.7.1.177 created 2012]

EC 2.7.1.178

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, GTD, KEGG, 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]

[EC 2.7.1.178 created 2013]

EC 2.7.1.179

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, GTD, KEGG, 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]

[EC 2.7.1.179 created 2013]

EC 2.7.1.180

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, 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]

[EC 2.7.1.180 created 2013, modified 2018]

EC 2.7.1.181

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, 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]

[EC 2.7.1.181 created 2014, modified 2017]

EC 2.7.1.182

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]

[EC 2.7.1.182 created 2014]

EC 2.7.1.183

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, 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]

[EC 2.7.1.183 created 2014]

EC 2.7.1.184

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, 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]

[EC 2.7.1.184 created 2014]

EC 2.7.1.185

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, 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]

[EC 2.7.1.185 created 2014]

EC 2.7.1.186

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]

[EC 2.7.1.186 created 2014]

EC 2.7.1.187

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, 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]

[EC 2.7.1.187 created 2015]

EC 2.7.1.188

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]

[EC 2.7.1.188 created 2015]

EC 2.7.1.189

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, 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]

[EC 2.7.1.189 created 2015]

EC 2.7.1.190

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, 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]

[EC 2.7.1.190 created 2015]

EC 2.7.1.191

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]

[EC 2.7.1.191 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.191]

EC 2.7.1.192

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]

[EC 2.7.1.192 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.192]

EC 2.7.1.193

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]

[EC 2.7.1.193 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.193]

EC 2.7.1.194

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]

[EC 2.7.1.194 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.194]

EC 2.7.1.195

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]

[EC 2.7.1.195 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.195]

EC 2.7.1.196

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]

[EC 2.7.1.196 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.196]

EC 2.7.1.197

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]

[EC 2.7.1.197 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.197]

EC 2.7.1.198

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]

[EC 2.7.1.198 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.198]

EC 2.7.1.199

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]

[EC 2.7.1.199 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.199]

EC 2.7.1.200

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]

[EC 2.7.1.200 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.200]

EC 2.7.1.201

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]

[EC 2.7.1.201 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.201]

EC 2.7.1.202

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]

[EC 2.7.1.202 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.202]

EC 2.7.1.203

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]

[EC 2.7.1.203 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.203]

EC 2.7.1.204

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]

[EC 2.7.1.204 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.204]

EC 2.7.1.205

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]

[EC 2.7.1.205 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.205]

EC 2.7.1.206

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]

[EC 2.7.1.206 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.206]

EC 2.7.1.207

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]

[EC 2.7.1.207 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.207]

EC 2.7.1.208

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]

[EC 2.7.1.208 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.208]

EC 2.7.1.209

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]

[EC 2.7.1.209 created 2016, modified 2018]

EC 2.7.1.210

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]

[EC 2.7.1.210 created 2016]

EC 2.7.1.211

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]

[EC 2.7.1.211 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.211]

EC 2.7.1.212

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]

[EC 2.7.1.212 created 2016]

EC 2.7.1.213

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, 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]

[EC 2.7.1.213 created 2016]

EC 2.7.1.214

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]

[EC 2.7.1.214 created 2016]

EC 2.7.1.215

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]

[EC 2.7.1.215 created 2016]

EC 2.7.1.216

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]

[EC 2.7.1.216 created 2017]

EC 2.7.1.217

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, 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]

[EC 2.7.1.217 created 2017]

EC 2.7.1.218

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]

[EC 2.7.1.218 created 2017]

EC 2.7.1.219

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, 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]

[EC 2.7.1.219 created 2017]

EC 2.7.1.220

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]

[EC 2.7.1.220 created 2017]

EC 2.7.1.221

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]

[EC 2.7.1.221 created 2017]

EC 2.7.1.222

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.

[EC 2.7.1.222 created 2017]

EC 2.7.1.223

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, 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]

[EC 2.7.1.223 created 2018]

EC 2.7.1.224

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]

[EC 2.7.1.224 created 2018]

EC 2.7.1.225

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, 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]

[EC 2.7.1.225 created 2019]

EC 2.7.1.226

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, 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]

[EC 2.7.1.226 created 2019]


Continued with EC 2.7.2 to EC 2.7.6
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