EC number:2.1.1.132

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.132
Description:Precorrin-6B C(5,15)-methyltransferase (decarboxylating).
Alternative Name: Precorrin-6Y methylase.
Precorrin-6Y C(5,15)-methyltransferase (decarboxylating).
Precorrin-6 methyltransferase.
Cath: 3.30.950.10; 3.40.1010.10; 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.132
BRENDA Enzyme Link: BRENDA 2.1.1.132
KEGG Enzyme Link: KEGG2.1.1.132
BioCyc Enzyme Link: BioCyc 2.1.1.132
ExPASy Enzyme Link: ExPASy2.1.1.132
EC2PDB Enzyme Link: EC2PDB 2.1.1.132
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.132
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.132
IntEnz Enzyme Link: IntEnz 2.1.1.132
MEDLINE Enzyme Link: MEDLINE 2.1.1.132

EC number:2.1.1.132

MSA:

2.1.1.132;
Phylogenetic Tree:

2.1.1.132;
Uniprot:
M-CSA:
RHEA:17477 precorrin-6B + 2 S-adenosyl-L-methionine = CO2 + 3 H(+) + precorrin-8X + 2 S-adenosyl-L-homocysteine
RULE(radius=1)
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis.Deery E, Schroeder S, Lawrence AD, Taylor SL, Seyedarabi A, Waterman J, Wilson KS, Brown D, Geeves MA, Howard MJ, Pickersgill RW, Warren MJ2012 Nov23042036
Biosynthesis of vitamin B12 in Pseudomonas denitrificans: the biosynthetic sequence from precorrin-6y to precorrin-8x is catalyzed by the cobL gene product.Blanche F, Famechon A, Thibaut D, Debussche L, Cameron B, Crouzet J1992 Feb1732195
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