EC number:2.7.1.49

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.49
Description:Hydroxymethylpyrimidine kinase.
Cath: 3.40.1190.20; 1.20.910.10; 3.40.225.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.49
BRENDA Enzyme Link: BRENDA 2.7.1.49
KEGG Enzyme Link: KEGG2.7.1.49
BioCyc Enzyme Link: BioCyc 2.7.1.49
ExPASy Enzyme Link: ExPASy2.7.1.49
EC2PDB Enzyme Link: EC2PDB 2.7.1.49
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.49
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.49
IntEnz Enzyme Link: IntEnz 2.7.1.49
MEDLINE Enzyme Link: MEDLINE 2.7.1.49

EC number:2.7.1.49

MSA:

2.7.1.49;
Phylogenetic Tree:

2.7.1.49;
Uniprot:
M-CSA:
RHEA:23096 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 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
Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase.Park JH, Burns K, Kinsland C, Begley TP2004 Mar14973012
Cloning and characterization of the thiD/J gene of Escherichia coli encoding a thiamin-synthesizing bifunctional enzyme, hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase.Mizote T, Tsuda M, Smith DD, Nakayama H, Nakazawa T1999 Feb10075431