ID   ADH7_YEAST              Reviewed;         361 AA.
AC   P25377;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-NOV-2008, entry version 65.
DE   RecName: Full=NADP-dependent alcohol dehydrogenase 7;
DE            EC=1.1.1.2;
DE   AltName: Full=NADP-dependent alcohol dehydrogenase VII;
DE            Short=ADHVII;
GN   Name=ADH7; OrderedLocusNames=YCR105W;
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=92244356; PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
RA   Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
RA   Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
RA   Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
RA   Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
RA   de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
RA   Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
RA   Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
RA   Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
RA   Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
RA   Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
RA   Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
RA   Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
RA   van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
RA   Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
RA   Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [2]
RP   CHARACTERIZATION, AND SUBUNIT.
RX   PubMed=12423374; DOI=10.1046/j.1432-1033.2002.03296.x;
RA   Larroy C., Pares X., Biosca J.A.;
RT   "Characterization of a Saccharomyces cerevisiae NADP(H)-dependent
RT   alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol
RT   dehydrogenase family.";
RL   Eur. J. Biochem. 269:5738-5745(2002).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC   -!- FUNCTION: NADP-dependent alcohol dehydrogenase with a broad
CC       substrate specificity.
CC   -!- CATALYTIC ACTIVITY: An alcohol + NADP(+) = an aldehyde + NADPH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: Present with 2870 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; X59720; CAA42237.1; -; Genomic_DNA.
DR   PIR; S19417; S19417.
DR   RefSeq; NP_010030.1; -.
DR   Ensembl; YCR105W; Saccharomyces cerevisiae.
DR   GeneID; 850469; -.
DR   GenomeReviews; X59720_GR; YCR105W.
DR   KEGG; sce:YCR105W; -.
DR   NMPDR; fig|4932.3.peg.760; -.
DR   CYGD; YCR105w; -.
DR   SGD; S000000702; ADH7.
DR   HOGENOM; P25377; -.
DR   LinkHub; P25377; -.
DR   NextBio; 966116; -.
DR   GermOnline; YCR105W; Saccharomyces cerevisiae.
DR   GO; GO:0005625; C:soluble fraction; IDA:SGD.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006066; P:cellular alcohol metabolic process; IDA:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
DR   InterPro; IPR013154; AlcDHase_GroES-like.
DR   InterPro; IPR002085; AlcDHase_SF_Zn.
DR   InterPro; IPR013149; AlcDHase_Zn-bd.
DR   InterPro; IPR002328; AlcDHase_Zn_CS.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Metal-binding; NADP; Oxidoreductase;
KW   Phosphoprotein; Zinc.
FT   CHAIN         1    361       NADP-dependent alcohol dehydrogenase 7.
FT                                /FTId=PRO_0000160735.
FT   METAL        46     46       Zinc 1; catalytic (By similarity).
FT   METAL        68     68       Zinc 1; catalytic (By similarity).
FT   METAL       100    100       Zinc 2 (By similarity).
FT   METAL       103    103       Zinc 2 (By similarity).
FT   METAL       106    106       Zinc 2 (By similarity).
FT   METAL       114    114       Zinc 2 (By similarity).
FT   METAL       164    164       Zinc 1; catalytic (By similarity).
FT   MOD_RES     316    316       Phosphoserine.
SQ   SEQUENCE   361 AA;  39348 MW;  BFB0E6C5F93D3F07 CRC64;
     MLYPEKFQGI GISNAKDWKH PKLVSFDPKP FGDHDVDVEI EACGICGSDF HIAVGNWGPV
     PENQILGHEI IGRVVKVGSK CHTGVKIGDR VGVGAQALAC FECERCKSDN EQYCTNDHVL
     TMWTPYKDGY ISQGGFASHV RLHEHFAIQI PENIPSPLAA PLLCGGITVF SPLLRNGCGP
     GKRVGIVGIG GIGHMGILLA KAMGAEVYAF SRGHSKREDS MKLGADHYIA MLEDKGWTEQ
     YSNALDLLVV CSSSLSKVNF DSIVKIMKIG GSIVSIAAPE VNEKLVLKPL GLMGVSISSS
     AIGSRKEIEQ LLKLVSEKNV KIWVEKLPIS EEGVSHAFTR MESGDVKYRF TLVDYDKKFH
     K
//