InterPro : IPR006538

Name  Cobalt chelatase, CobT subunit Short Name  CobT
Type  Family Description  These proteins are CobT subunits of the aerobic cobalt chelatase (aerobic cobalamin biosynthesis pathway). Pseudomonas denitrificansCobT has been experimentally characterised [, ]. Aerobic cobalt chelatase consists of three subunits, CobT, CobN () and CobS ().Cobalamin (vitamin B12) can be complexed with metal via the ATP-dependent reactions (aerobic pathway) (e.g., in P. denitrificans) or via ATP-independent reactions (anaerobic pathway) (e.g., in Salmonella typhimurium) [, ]. The corresponding cobalt chelatases are not homologous. However, aerobic cobalt chelatase subunits CobN and CobS are homologous to Mg-chelatase subunits BchH and BchI, respectively []. CobT, too, has been found to be remotely related to the third subunit of Mg-chelatase, BchD (involved in bacteriochlorophyll synthesis, e.g., in Rhodobacter capsulatus) [].Nomenclature note: CobT of the aerobic pathway P. denitrificans is not a homologue of CobT of the anaerobic pathway (Salmonella typhimurium, Escherichia coli). Therefore, annotation of any members of this family as nicotinate-mononucleotide--5,6-dimethylbenzimidazole phosphoribosyltransferases is erroneous.
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR002035 von Willebrand factor, type A VWF_A Domain

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Roth JR Cobalamin (coenzyme B12): synthesis and biological significance. 1996 Annu Rev Microbiol 50 137-81
Debussche L Assay, purification, and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans. 1992 J Bacteriol 174 7445-51
Cameron B Genetic and sequence analyses of a Pseudomonas denitrificans DNA fragment containing two cob genes. 1991 J Bacteriol 173 6058-65
Fodje MN Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase. 2001 J Mol Biol 311 111-22



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)