EC number:2.7.7.93

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.93
Description:Phosphonoformate cytidylyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.93
BRENDA Enzyme Link: BRENDA 2.7.7.93
KEGG Enzyme Link: KEGG2.7.7.93
BioCyc Enzyme Link: BioCyc 2.7.7.93
ExPASy Enzyme Link: ExPASy2.7.7.93
EC2PDB Enzyme Link: EC2PDB 2.7.7.93
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.93
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.93
IntEnz Enzyme Link: IntEnz 2.7.7.93
MEDLINE Enzyme Link: MEDLINE 2.7.7.93

EC number:2.7.7.93

MSA:

2.7.7.93;
Phylogenetic Tree:

2.7.7.93;
Uniprot:
M-CSA:
RHEA:49428 CTP + phosphonoformate = CMP-5'-phosphonoformate + diphosphate
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
Unusual transformations in the biosynthesis of the antibiotic phosphinothricin tripeptide.Blodgett JA, Thomas PM, Li G, Velasquez JE, van der Donk WA, Kelleher NL, Metcalf WW2007 Aug17632514