Protein Family Models

This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA Swiss:P29946 and CbiP Swiss:Q05597 from S.typhimurium [4], and CobQ Swiss:Q52686 from R. capsulatus [3]. These amidases catalyse amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria [4]. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family [6]. [1]. 9742225. Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon. Raux E, Lanois A, Warren MJ, Rambach A, Thermes C;. Biochem J 1998;335:159-166. [2]. 9742226. Cobalamin (vitamin B12) biosynthesis: functional characterization of the Bacillus megaterium cbi genes required to convert uroporphyrinogen III into cobyrinic acid a,c-diamide. Raux E, Lanois A, Rambach A, Warren MJ, Thermes C;. Biochem J 1998;335:167-173. [3]. 7635831. Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus. Pollich M, Klug G;. J Bacteriol 1995;177:4481-4487. [4]. 8501034. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM;. J Bacteriol 1993;175:3303-3316. [5]. 10966576. The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of AT. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

hydrogenobyrinic/cobyrinic acid a,c-diamide synthase catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate or cobyrinate, using either L-glutamine or ammonia as the nitrogen source

Date:

2017-06-05

Responsible for the amidation of carboxylic groups at position A and C of cobyrinic acid or hydrogenobrynic acid

Date:

2021-07-22

Members of this family are the cobyrinic acid a,c-diamide synthetase (EC 6.3.5.11) CbiA for anaerobic biosynthesis of cobalamin or the hydrogenobyrinic acid a,c-diamide synthase (EC 6.3.5.9) CobB for aerobic biosynthesis of the same. Some archaeal CbiA have a second function as Ni-sirohydrochlorin a,c-diamide synthase (EC 6.3.5.12) for F(430) biosynthesis. Each of these enzymes is responsible for the amidation of carboxylic groups at positions A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP hydrogenolyzed for each amidation.

Gene:

cobB

Date:

2024-07-08