ID   DHSO2_YEAST             Reviewed;         357 AA.
AC   Q07786;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Sorbitol dehydrogenase 2;
DE            EC=1.1.1.14;
DE   AltName: Full=L-iditol 2-dehydrogenase 2;
GN   Name=SOR2; OrderedLocusNames=YDL246C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
CC   -!- CATALYTIC ACTIVITY: L-iditol + NAD(+) = L-sorbose + NADH.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- INTERACTION:
CC       P02829:HSP82; NbExp=1; IntAct=EBI-33572, EBI-8659;
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; Z74294; CAA98826.1; -; Genomic_DNA.
DR   PIR; S67811; S67811.
DR   RefSeq; NP_010035.1; -.
DR   HSSP; O96496; 1E3J.
DR   DIP; DIP:1512N; -.
DR   IntAct; Q07786; 10.
DR   Ensembl; YDL246C; Saccharomyces cerevisiae.
DR   GeneID; 851351; -.
DR   GenomeReviews; Z71256_GR; YDL246C.
DR   KEGG; sce:YDL246C; -.
DR   NMPDR; fig|4932.3.peg.767; -.
DR   CYGD; YDL246c; -.
DR   SGD; S000002405; SOR2.
DR   HOGENOM; Q07786; -.
DR   BRENDA; 1.1.1.14; 250.
DR   NextBio; 968441; -.
DR   GermOnline; YDL246C; Saccharomyces cerevisiae.
DR   GO; GO:0003939; F:L-iditol 2-dehydrogenase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR013149; ADH_Zn-bd.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   ProDom; PD040557; GroES_related; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    357       Sorbitol dehydrogenase 2.
FT                                /FTId=PRO_0000160822.
FT   METAL        43     43       Zinc; catalytic (By similarity).
FT   METAL        68     68       Zinc; catalytic (By similarity).
FT   METAL        69     69       Zinc; catalytic (By similarity).
SQ   SEQUENCE   357 AA;  38097 MW;  1684792040A3834A CRC64;
     MSQNSNPAVV LEKVGDIAIE QRPIPTIKDP HYVKLAIKAT GICGSDIHYY RSGGIGKYIL
     KAPMVLGHES SGQVVEVGDA VTRVKVGDRV AIEPGVPSRY SDETKEGSYN LCPHMAFAAT
     PPIDGTLVKY YLSPEDFLVK LPEGVSYEEG ACVEPLSVGV HSNKLAGVRF GTKVVVFGAG
     PVGLLTGAVA RAFGATDVIF VDVFDNKLQR AKDFGATNTF NSSQFSTDKA QDLADGVQKL
     LGGNHADVVF ECSGADVCID AAVKTTKVGG TMVQVGMGKN YTNFPIAEVS GKEMKLIGCF
     RYSFGDYRDA VNLVATGKVN VKPLITHKFK FEDAAKAYDY NIAHGGEVVK TIIFGPE
//