EC number:2.1.1.289

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.289
Description:Cobalt-precorrin-7 (C(5))-methyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.289
BRENDA Enzyme Link: BRENDA 2.1.1.289
KEGG Enzyme Link: KEGG2.1.1.289
BioCyc Enzyme Link: BioCyc 2.1.1.289
ExPASy Enzyme Link: ExPASy2.1.1.289
EC2PDB Enzyme Link: EC2PDB 2.1.1.289
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.289
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.289
IntEnz Enzyme Link: IntEnz 2.1.1.289
MEDLINE Enzyme Link: MEDLINE 2.1.1.289

EC number:2.1.1.289

MSA:

2.1.1.289;
Phylogenetic Tree:

2.1.1.289;
Uniprot:
M-CSA:
RHEA:34591 Co-precorrin-7 + S-adenosyl-L-methionine = Co-precorrin-8X + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[CH;+0:2]=[*:3].[*:4]-[S+;H0:5](-[*:6])-[CH3;+0:7]>>[*:1]-[C;H0;+0:2](=[*:3])-[CH3;+0:7].[*:4]-[S;H0;+0:5]-[*:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF2002 Nov12429089
Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway.Santander PJ, Kajiwara Y, Williams HJ, Scott AI2006 Feb 116198574