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Cobaltochelatase CobS subunit N terminal
This domain family is found in bacteria, and is approximately 40 amino acids in length. The family is found in association with Pfam:PF07728. There are two completely conserved residues (P and F) that may be functionally important. This family is the N terminal of the CobS subunit of cobaltochelatase. Cobaltochelatase belongs to the AAA+ superfamily of proteins. CobS and CobT form a chaperone like complex. [1]. 19545636. The AAA(+) motor complex of subunits CobS and CobT of cobaltochelatase visualized by single particle electron microscopy. Lundqvist J, Elmlund D, Heldt D, Deery E, Soderberg CA, Hansson M, Warren M, Al-Karadaghi S;. J Struct Biol. 2009;167:227-234. (from Pfam)
AAA family ATPase
This Pfam entry includes some of the AAA proteins not detected by the Pfam:PF00004 model. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)
cobaltochelatase subunit CobS
This model describes CobS, as the term is used in Pseudomonas denitrificans. It is a subunit of the heterotrimeric, ATP-dependent enzyme that catalyzes cobalt insertion during aerobic cobalamin biosynthesis. The other two subunits are CobT (TIGR01651) and CobN (PF02514 CobN/Magnesium Chelatase) proteins. Note that this CobS protein is not related to the CobS from the anaerobic biosynthesis pathway found in Salmonella typhimurium, or to that protein's counterpart in Escherichia coli, which synthesizes cobalamin only when it is supplied with the precursor cobinamide, a complex intermediate.
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