ID ADH7_YEAST Reviewed; 361 AA.
AC P25377; D6VRA5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-APR-2013, entry version 105.
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 (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX 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 [5]
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 EMBL; BK006937; DAA07574.1; -; Genomic_DNA.
DR PIR; S19417; S19417.
DR RefSeq; NP_010030.1; NM_001178812.1.
DR ProteinModelPortal; P25377; -.
DR SMR; P25377; 1-359.
DR DIP; DIP-7661N; -.
DR MINT; MINT-2789097; -.
DR STRING; 4932.YCR105W; -.
DR PaxDb; P25377; -.
DR EnsemblFungi; YCR105W; YCR105W; YCR105W.
DR GeneID; 850469; -.
DR KEGG; sce:YCR105W; -.
DR CYGD; YCR105w; -.
DR SGD; S000000702; ADH7.
DR eggNOG; COG1064; -.
DR GeneTree; ENSGT00550000075527; -.
DR HOGENOM; HOG000294667; -.
DR KO; K00002; -.
DR OMA; DYILDTV; -.
DR OrthoDB; EOG40ZV6H; -.
DR NextBio; 966116; -.
DR Genevestigator; P25377; -.
DR GermOnline; YCR105W; Saccharomyces cerevisiae.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:SGD.
DR GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:SGD.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR013149; ADH_C.
DR InterPro; IPR013154; ADH_GroES-like.
DR InterPro; IPR002085; ADH_SF_Zn-type.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR InterPro; IPR011032; GroES-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR11695; PTHR11695; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES_like; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Metal-binding; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1 361 NADP-dependent alcohol dehydrogenase 7.
FT /FTId=PRO_0000160735.
FT NP_BIND 188 193 NAD (By similarity).
FT NP_BIND 276 278 NAD (By similarity).
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 BINDING 216 216 NAD (By similarity).
FT BINDING 349 349 NAD (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
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