Accession | TIGR00636 |
Name | PduO_Nterm |
Function | ATP:cob(I)alamin adenosyltransferase |
Trusted Cutoff | 108.45 |
Domain Trusted Cutoff | 108.45 |
Noise Cutoff | 53.90 |
Domain Noise Cutoff | 53.90 |
Isology Type | equivalog_domain |
EC Number | 2.5.1.17 |
HMM Length | 171 |
Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
Subrole Category | Heme, porphyrin, and cobalamin |
Gene Ontology Term | GO:0008817: cob(I)yrinic acid a,c-diamide adenosyltransferase activity molecular_function |
| GO:0009236: cobalamin biosynthetic process biological_process |
Author | Haft DH |
Entry Date | Oct 25 1999 11:40AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This HMM represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens. |
References | RN [1]
RM 11160088
RT Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene.
RA Johnson CL, Pechonick E, Park SD, Havemann GD, Leal NA, Bobik TA.
RL J Bacteriol 2001 Mar;183(5):1577-84
RN [2]
RM PMID: 15687219
RT Identification of genes involved in the glyoxylate regeneration cycle in Methylobacterium extorquens AM1, including two new genes, meaC and meaD.
RA Korotkova N, Lidstrom ME, Chistoserdova L
RL J Bacteriol. 2005 Feb;187(4):1523-6. |
Genome Property | GenProp0269: coenzyme B12 biosynthesis from cob(II)yrinate diamide (HMM) |