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magnesium chelatase domain-containing protein
Magnesium chelatase, subunit ChlI C-terminal
This is a family of the C-terminal of putative bacterial magnesium chelatase subunit ChlI proteins. Most members have the associated Pfam:PF01078. (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)
ATP-binding protein
Magnesium-chelatase is a three-component enzyme that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa. [1]. 9359397. Mechanism and regulation of Mg-chelatase. Walker CJ, Willows RD;. Biochem J 1997;327:321-333. [2]. 9457877. Reconstitution of an active magnesium chelatase enzyme complex from the bchI, -D, and -H gene products of the green sulfur bacterium Chlorobium vibrioforme expressed in Escherichia coli. Petersen BL, Jensen PE, Gibson LC, Stummann BM, Hunter CN, Henningsen KW;. J Bacteriol 1998;180:699-704. (from Pfam)
MCM P-loop domain
YifB family Mg chelatase-like AAA ATPase
YifB family Mg chelatase-like AAA ATPase with an AAA (ATPases Associated with various cellular Activities) domain
Members of this family are AAA family ATPases, more similar to magnesium chelatase than to Lon protease, but are not magnesium chelatase. Members include proteins called YifB in Escherichia coli K-12 and ComM in Haemophilus influenzae. The function is unknown.
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