EC number:2.7.1.185

Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.185
Description:Mevalonate 3-kinase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.185
BRENDA Enzyme Link: BRENDA 2.7.1.185
KEGG Enzyme Link: KEGG2.7.1.185
BioCyc Enzyme Link: BioCyc 2.7.1.185
ExPASy Enzyme Link: ExPASy2.7.1.185
EC2PDB Enzyme Link: EC2PDB 2.7.1.185
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.185
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.185
IntEnz Enzyme Link: IntEnz 2.7.1.185
MEDLINE Enzyme Link: MEDLINE 2.7.1.185

EC number:2.7.1.185

MSA:

2.7.1.185;
Phylogenetic Tree:

2.7.1.185;
Uniprot:
M-CSA:
RHEA:42884 (R)-mevalonate + ATP = (R)-3-phosphomevalonate + ADP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Evidence of a novel mevalonate pathway in archaea.Vinokur JM, Korman TP, Cao Z, Bowie JU2014 Jul 124914732
(R)-mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum.Azami Y, Hattori A, Nishimura H, Kawaide H, Yoshimura T, Hemmi H2014 Jun 624755225