EC number:2.1.1.258

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.258
Description:Co-methyltransferase.
Cath: 3.20.20.20;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.258
BRENDA Enzyme Link: BRENDA 2.1.1.258
KEGG Enzyme Link: KEGG2.1.1.258
BioCyc Enzyme Link: BioCyc 2.1.1.258
ExPASy Enzyme Link: ExPASy2.1.1.258
EC2PDB Enzyme Link: EC2PDB 2.1.1.258
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.258
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.258
IntEnz Enzyme Link: IntEnz 2.1.1.258
MEDLINE Enzyme Link: MEDLINE 2.1.1.258

EC number:2.1.1.258

MSA:

2.1.1.258;
Phylogenetic Tree:

2.1.1.258;
Uniprot:
M-CSA:
RHEA:45200 (6S)-5,6,7,8-tetrahydrofolate + [methyl-Co(III) corrinoid Fe-S protein] = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + [Co(I) corrinoid Fe-S protein] + H(+)
RULE(radius=1) [*:1]-[NH;+0:2]-[*:3].[CH3;+0:4]-[Co+2;H0:5]>>[*:1]-[N;H0;+0:2](-[*:3])-[CH3;+0:4].[Co+;H0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum.Roberts DL, Zhao S, Doukov T, Ragsdale SW1994 Oct7928975
Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases.Doukov TI, Hemmi H, Drennan CL, Ragsdale SW2007 Mar 217172470
Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW2000 Aug 1510997901