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CobQ/CobB/MinD/ParA nucleotide binding domain
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 . TRUNCATED at 1650 bytes (from Pfam)
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family
nitrogenase iron protein
This HMM describes nitrogenase (EC 1.18.6.1) iron protein, also called nitrogenase reductase or nitrogenase component II. This model includes molybdenum-iron nitrogenase reductase (nifH), vanadium-iron nitrogenase reductase (vnfH), and iron-iron nitrogenase reductase (anfH). The model excludes the homologous protein from the light-independent protochlorophyllide reductase.
nitrogenase iron protein NifH is the component II of nitogenase, which is responsible for the biological nitrogen fixation (reduction of molecular nitrogen to ammonia) in an ATP-dependent process
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