ID ARDH_CANTR Reviewed; 282 AA. AC P50166; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 50. DE RecName: Full=D-arabinitol 2-dehydrogenase [ribulose-forming]; DE Short=ARDH; DE EC=1.1.1.250; GN Name=ARD; OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; OC Candida. OX NCBI_TaxID=5482; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 750 / CBS 94 / DSM 11953 / JCM 1541; RX MEDLINE=95212917; PubMed=7698655; DOI=10.1016/0378-1119(94)00900-D; RA Murray J.S., Wong M.L., Miyada C.G., Switchenko A.C., Goodman T.C., RA Wong B.; RT "Isolation, characterization and expression of the gene that encodes RT D-arabinitol dehydrogenase in Candida tropicalis."; RL Gene 155:123-128(1995). RN [2] RP CHARACTERIZATION. RX MEDLINE=94071892; PubMed=8250887; DOI=10.1006/bbrc.1993.2397; RA Quong M.W., Miyada C.G., Switchenko A.C., Goodman T.C.; RT "Identification, purification, and characterization of a D-arabinitol- RT specific dehydrogenase from Candida tropicalis."; RL Biochem. Biophys. Res. Commun. 196:1323-1329(1993). CC -!- CATALYTIC ACTIVITY: D-arabinitol + NAD(+) = D-ribulose + NADH. CC -!- PATHWAY: Carbohydrate metabolism; D-arabinitol metabolism. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U00675; AAA66355.1; -; Genomic_DNA. DR PIR; JC4041; JC4041. DR HSSP; Q9ZFY9; 1FK8. DR BRENDA; 1.1.1.250; 1242. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0047038; F:D-arabinitol 2-dehydrogenase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002198; DH_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR19410; ADH_short_C2; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; NAD; Oxidoreductase. FT CHAIN 1 282 D-arabinitol 2-dehydrogenase [ribulose- FT forming]. FT /FTId=PRO_0000054518. FT NP_BIND 26 48 NAD (By similarity). FT ACT_SITE 185 185 Proton acceptor (By similarity). FT BINDING 170 170 Substrate (By similarity). SQ SEQUENCE 282 AA; 30748 MW; A82A3DA4E771EF0D CRC64; MDSSSYWSYD NIVPSFRLDG KLVIITGGSG GLSAVVSRAL LAKGADIALI DMNLERTQQA ARDVLQWGEE QMKGKHESPI GQVSAWSCNI GDAEAVELTF KAINEHHGKV ASVLINTAGY AENFPAEEYP AKNAENIMKV NGLGSFYVSQ AFARPLIQNN MTGSIILIGS MSGTIVNDPQ PQCMYNMSKA GVIHLARSLA CEWAKYNIRV NTLSPGYILT PLTRNVISGH TEMKTEWESK IPMKRMAEPK EFVGSILYLA SDSASSYTTG HNLVVDGGYE CW //