KEGG   ENZYME: 2.7.1.165Help
Entry
EC 2.7.1.165                Enzyme                                 

Name
glycerate 2-kinase;
D-glycerate-2-kinase;
glycerate kinase (2-phosphoglycerate forming);
ATP:(R)-glycerate 2-phosphotransferase
Class
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with an alcohol group as acceptor
BRITE hierarchy
Sysname
ATP:D-glycerate 2-phosphotransferase
Reaction(IUBMB)
ATP + D-glycerate = ADP + 2-phospho-D-glycerate [RN:R08572]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
D-glycerate [CPD:C00258]
Product
ADP [CPD:C00008];
2-phospho-D-glycerate [CPD:C00631]
Comment
A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea [1,2]. In the bacterium 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].
History
EC 2.7.1.165 created 2010
Pathway
Pentose phosphate pathway
Glycine, serine and threonine metabolism
Methane metabolism
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K11529  
glycerate 2-kinase
Genes
MEX: 
MEA: 
MDI: 
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TAC: 
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FAC: 
PHO: 
PAB: 
PFU: 
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PYN: 
PYA: 
PYS: 
TON: 
TGA: 
TGAM_1557(ttuD)
TSI: 
TBA: 
THE: 
THA: 
TLT: 
APE: 
ACJ: 
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IAG: 
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SACN: 
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AHO: 
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POG: 
CMA: 
TUZ: 
TTN: 
TTX_0788(garK)
VDI: 
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THB: 
ASC: 
CLG: 
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 » show all
Taxonomy
Reference
1  [PMID:19690808]
  Authors
Liu B, Wu L, Liu T, Hong Y, Shen Y, Ni J
  Title
A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.
  Journal
Biotechnol. Lett. 31 (2009) 1937-41.
  Organism
Sulfolobus tokodaii
  Sequence
[sto:ST2037]
Reference
2  [PMID:16684110]
  Authors
Reher M, Bott M, Schonheit P
  Title
Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus.
  Journal
FEMS. Microbiol. Lett. 259 (2006) 113-9.
  Organism
Picrophilus torridus
  Sequence
[pto:PTO1442]
Reference
3  [PMID:17563835]
  Authors
Liu B, Hong Y, Wu L, Li Z, Ni J, Sheng D, Shen Y
  Title
A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization.
  Journal
Extremophiles. 11 (2007) 733-9.
  Organism
Pyrococcus horikoshii
  Sequence
[pho:PH0495]
Reference
4
  Authors
Noh, M., Jung, J.H. and Lee, S.B.
  Title
Purification and characterization of glycerate kinase from the thermoacidophilic archaeon Thermoplasma acidophilum: an enzyme belonging to the second glycerate kinase family.
  Journal
Biotechnol. Bioprocess Eng. 11 (2006) 344-350.
Reference
5  [PMID:1336459]
  Authors
Yoshida T, Fukuta K, Mitsunaga T, Yamada H, Izumi Y
  Title
Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2.
  Journal
Eur. J. Biochem. 210 (1992) 849-54.
  Organism
Hyphomicrobium methylovorum
Reference
6  [PMID:9772162]
  Authors
Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA
  Title
Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli.
  Journal
Biochemistry. 37 (1998) 14369-75.
  Organism
Escherichia coli
  Sequence
[eco:b3124]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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