ID   ARDH_PICST              Reviewed;         278 AA.
AC   P50167; A3LUR3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=D-arabinitol 2-dehydrogenase [ribulose-forming];
DE            Short=ARDH;
DE            EC=1.1.1.250;
GN   Name=ARDH; Synonyms=ARD2; ORFNames=PICST_65696;
OS   Pichia stipitis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Pichia.
OX   NCBI_TaxID=4924;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545;
RX   MEDLINE=96090133; PubMed=7483848; DOI=10.1002/yea.320110906;
RA   Hallborn J., Walfridsson M., Penttilae M., Keraenen S.,
RA   Hahn-Haegerdal B.;
RT   "A short-chain dehydrogenase gene from Pichia stipitis having D-
RT   arabinitol dehydrogenase activity.";
RL   Yeast 11:839-847(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-
RT   fermenting yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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.
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DR   EMBL; Z46866; CAA86939.1; -; mRNA.
DR   EMBL; CP000499; ABN67006.1; -; Genomic_DNA.
DR   PIR; S57351; S57351.
DR   RefSeq; XP_001385035.1; -.
DR   HSSP; Q9ZFY9; 1FK8.
DR   GeneID; 4839199; -.
DR   KEGG; pic:PICST_65696; -.
DR   OMA; P50167; IVNDPQP.
DR   BRENDA; 1.1.1.250; 81766.
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   2: Evidence at transcript level;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    278       D-arabinitol 2-dehydrogenase [ribulose-
FT                                forming].
FT                                /FTId=PRO_0000054519.
FT   NP_BIND      22     44       NAD (By similarity).
FT   ACT_SITE    181    181       Proton acceptor (By similarity).
FT   BINDING     166    166       Substrate (By similarity).
SQ   SEQUENCE   278 AA;  30003 MW;  36869165F23964F6 CRC64;
     MDYSYANVVP NFRLDGRLAI ITGGSGGLAA VISRALLAQG ADVALIDMNL ERTKSAAKEV
     LGWGEETLKG EHASAIGQVS AWSCNIGDAE AVDATFSSIN EHHGKIADLL INTAGYCENF
     PAETYPATNA ESIMKVNGLG SFYVSQSFAR PLIQNNLRGS IILIGSMSGT IVNDPQPQCM
     YNMSKAGVIH LVRSLACEWA KYNIRVNTLS PGYILTPLTR NVISGHTEMK EAWESKIPMK
     RMAEPKEFVG SILYLASETA SSYTTGHNLV VDGGYECW
//