Enzyme

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     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.101
Description:Formylmethanofuran--tetrahydromethanopterin N-formyltransferase.
Cath: 3.30.70.520;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.101
BRENDA Enzyme Link: BRENDA 2.3.1.101
KEGG Enzyme Link: KEGG2.3.1.101
BioCyc Enzyme Link: BioCyc 2.3.1.101
ExPASy Enzyme Link: ExPASy2.3.1.101
EC2PDB Enzyme Link: EC2PDB 2.3.1.101
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.101
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.101
IntEnz Enzyme Link: IntEnz 2.3.1.101
MEDLINE Enzyme Link: MEDLINE 2.3.1.101
MSA:

2.3.1.101;

Phylogenetic Tree:

2.3.1.101;

Uniprot:
M-CSA:
RHEA:18061 5,6,7,8-tetrahydromethanopterin + H(+) + N-formylmethanofuran = methanofuran + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
RULE(radius=1) [*:1]-[NH;+0:2]-[*:3].[*:4]=[CH;+0:5]-[NH;+0:6]-[*:7].[H+;H0:8]>>[*:7]-[NH2;+0:6].[*:4]=[CH;+0:5]-[N;H0;+0:2](-[*:1])-[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide.Donnelly MI, Wolfe RS1986 Dec 153097011
Generation of formate by the formyltransferase/hydrolase complex (Fhc) from Methylobacterium extorquens AM1.Pomper BK, Saurel O, Milon A, Vorholt JA2002 Jul 1712123819
Characterization of the formyltransferase from Methylobacterium extorquens AM1.Pomper BK, Vorholt JA2001 Sep11532013