EC number:2.7.1.161

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:2.7.1.161
Description:CTP-dependent riboflavin kinase.
Cath: 1.10.10.10; 2.40.30.30;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.161
BRENDA Enzyme Link: BRENDA 2.7.1.161
KEGG Enzyme Link: KEGG2.7.1.161
BioCyc Enzyme Link: BioCyc 2.7.1.161
ExPASy Enzyme Link: ExPASy2.7.1.161
EC2PDB Enzyme Link: EC2PDB 2.7.1.161
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.161
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.161
IntEnz Enzyme Link: IntEnz 2.7.1.161
MEDLINE Enzyme Link: MEDLINE 2.7.1.161

EC number:2.7.1.161

MSA:

2.7.1.161;
Phylogenetic Tree:

2.7.1.161;
Uniprot:
M-CSA:
RHEA:25021 CTP + riboflavin = CDP + FMN + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification and characterization of an archaeon-specific riboflavin kinase.Mashhadi Z, Zhang H, Xu H, White RH2008 Apr18245297
A CTP-dependent archaeal riboflavin kinase forms a bridge in the evolution of cradle-loop barrels.Ammelburg M, Hartmann MD, Djuranovic S, Alva V, Koretke KK, Martin J, Sauer G, Truffault V, Zeth K, Lupas AN, Coles M2007 Dec18073108