EC 2 - Transferases
EC 2.7 - Transferring phosphorus-containing groups
EC 2.7.1 - Phosphotransferases with an alcohol group as acceptor
EC 2.7.1.165 - Glycerate 2-kinase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 2.7.1.165
Names
Accepted name:
glycerate 2-kinase
Other
names:
D-glycerate-2-kinase
glycerate kinase (2-phosphoglycerate forming)
glycerate kinase (2-phosphoglycerate forming)
Systematic name:
ATP:D-glycerate 2-phosphotransferase
Reaction
- ATP + D-glycerate = ADP + 2-phospho-D-glycerate
Cofactor
Comments:
A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea [1,2]. In Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assaimilation 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
Protein domains and families:
PROSITE:PDOC00706
Gene Ontology:
GO:0043798
UniProtKB/Swiss-Prot:
References
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A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.Biotechnol. Lett. 31 : 1937-1941 (2009). [PMID: 19690808]
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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 : 113-119 (2006). [PMID: 16684110]
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A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization.Extremophiles 11 : 733-739 (2007). [PMID: 17563835]
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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 : 344-350 (2006).
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Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2.Eur. J. Biochem. 210 : 849-854 (1992). [PMID: 1336459]
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Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli.Biochemistry 37 : 14369-14375 (1998). [PMID: 9772162]
[EC 2.7.1.165 created 2010]