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AAA family ATPase
This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop. (from Pfam)
ArsA-related P-loop ATPase
This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell. [1]. 1704144. The plasmid-encoded arsenical resistance pump: an. anion-translocating ATPase.. Rosen BP;. Res Microbiol 1990;141:336-341. (from Pfam)
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)
arsenical pump-driving ATPase
The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).
TRC40/GET3/ArsA family transport-energizing ATPase
Members of this family are ATPases that energize transport, although with different partner proteins for different functions. Recent findings show that TRC40 (GET3 in yeast) in involved in the insertion of tail-anchored membrane proteins in eukaryotes. A similar function is expected for members of this family in archaea. However, the earliest discovery of a function for this protein family is ArsA, an arsenic resistance protein that partners with ArsB (see PF02040) for As(III) efflux.
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