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HAD hydrolase-like protein
Polynucleotide kinase 3 phosphatase
Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin [1]. [1]. 11729194. Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by gamma-radiation or camptothecin in Schizosaccharomyces pombe. Meijer M, Karimi-Busheri F, Huang TY, Weinfeld M, Young D;. J Biol Chem. 2002;277:4050-4055. [2]. 12056900. Purification and partial characterization of a DNA 3'-phosphatase from Schizosaccharomyces pombe. Jilani A, Ramotar D;. Biochemistry. 2002;41:7688-7694. [3]. 11278831. Uncoupling of 3'-phosphatase and 5'-kinase functions in budding yeast. Characterization of Saccharomyces cerevisiae DNA 3'-phosphatase (TPP1). Vance JR, Wilson TE;. J Biol Chem. 2001;276:15073-15081. [4]. 10446193. Molecular characterization of a human DNA kinase. Karimi-Busheri F, Daly G, Robins P, Canas B, Pappin DJ, Sgouros J, Miller GG, Fakhrai H, Davis EM, Le Beau MM, Weinfeld M;. J Biol Chem. 1999;274:24187-24194. (from Pfam)
Imidazoleglycerol-phosphate dehydratase
bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase
bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate and the hydrolysis of L-histidinol phosphate to L-histidinol and phosphate
imidazoleglycerol-phosphate dehydratase HisB
HAD-IIIA family hydrolase
This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261, [3]) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme.
histidinol-phosphate phosphatase domain
This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.
histidinol-phosphatase
This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis.
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB
Catalyzes the formation of 3-(imidazol-4-yl)-2-oxopropyl phosphate from D-ethythro-1-(imidazol-4-yl)glycerol 3-phosphate and histidinol from histidinol phosphate
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