{PDOC00061} {PS00798; ALDOKETO_REDUCTASE_1} {PS00062; ALDOKETO_REDUCTASE_2} {PS00063; ALDOKETO_REDUCTASE_3} {BEGIN} ***************************************** * Aldo/keto reductase family signatures * ***************************************** The aldo-keto reductase family [1,2] groups together a number of structurally and functionally related NADPH-dependent oxidoreductases as well as some other proteins. The proteins known to belong to this family are: - Aldehyde reductase (EC 1.1.1.2). - Aldose reductase (EC 1.1.1.21). - 3-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.50), which terminates androgen action by converting 5-alpha-dihydrotestosterone to 3-alpha- androstanediol. - Prostaglandin F synthase (EC 1.1.1.188) which catalyzes the reduction of prostaglandins H2 and D2 to F2-alpha. - D-sorbitol-6-phosphate dehydrogenase (EC 1.1.1.200) from apple. - Morphine 6-dehydrogenase (EC 1.1.1.218) from Pseudomonas putida plasmid pMDH7.2 (gene morA). - Chlordecone reductase (EC 1.1.1.225) which reduces the pesticide chlordecone (kepone) to the corresponding alcohol. - 2,5-diketo-D-gluconic acid reductase (EC 1.1.1.274) which catalyzes the reduction of 2,5-diketogluconic acid to 2-keto-L-gulonic acid, a key intermediate in the production of ascorbic acid. - NAD(P)H-dependent xylose reductase (EC 1.1.1.-) from the yeast Pichia stipitis. This enzyme reduces xylose into xylit. - Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC 1.3.1.20). - 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.99.6) which catalyzes the reduction of delta(4)-3-oxosteroids. - A soybean reductase, which co-acts with chalcone synthase in the formation of 4,2',4'-trihydroxychalcone. - Frog eye lens rho crystallin. - Yeast GCY protein, whose function is not known. - Leishmania major P110/11E protein. P110/11E is a developmentally regulated protein whose abundance is markedly elevated in promastigotes compared with amastigotes. Its exact function is not yet known. - Escherichia coli hypothetical protein yafB. - Escherichia coli hypothetical protein yghE. - Yeast hypothetical protein YBR149w. - Yeast hypothetical protein YHR104w. - Yeast hypothetical protein YJR096w. These proteins have all about 300 amino acid residues. We derived 3 consensus patterns specific to this family of proteins. The first one is located in the N-terminal section of these proteins. The second pattern is located in the central section. The third pattern, located in the C-terminal, is centered on a lysine residue whose chemical modification, in aldose and aldehyde reductases, affect the catalytic efficiency. -Consensus pattern: G-[FY]-R-[HSAL]-[LIVMF]-D-[STAGCL]-[AS]-x(5)-[EQ]-x(2)- [LIVMCA]-[GS] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Consensus pattern: [LIVMFY]-x(8)-{L}-[KREQ]-{K}-[LIVM]-G-[LIVM]-[SC]-N-[FY] -Sequences known to belong to this class detected by the pattern: ALL, except for morA. -Other sequence(s) detected in Swiss-Prot: 5. -Consensus pattern: [LIVM]-[PAIV]-[KR]-[ST]-{EPQG}-{RFI}-x(2)-R-{SVAF}-x- [GSTAEQK]-[NSL]-x-{LVRI}-[LIVMFA] [K may be the active site residue] -Sequences known to belong to this class detected by the pattern: ALL, except for yafB. -Other sequence(s) detected in Swiss-Prot: 41. -Last update: April 2006 / Patterns revised. [ 1] Bohren K.M., Bullock B., Wermuth B., Gabbay K.H. "The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases." J. Biol. Chem. 264:9547-9551(1989). PubMed=2498333 [ 2] Bruce N.C., Willey D.L., Coulson A.F.M., Jeffery J. "Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities." Biochem. J. 299:805-811(1994). PubMed=8192670 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}