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   27-MAR-2024, entry version 178.
DE   RecName: Full=NADP-dependent alcohol dehydrogenase 7;
DE            EC=1.1.1.2 {ECO:0000269|PubMed:12423374};
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; Saccharomycetes;
OC   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., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., 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., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   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;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 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 alcohol
RT   dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase
RT   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., Dephoure N.,
RA   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 IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC   -!- FUNCTION: NADP-dependent alcohol dehydrogenase with a broad substrate
CC       specificity. The oxidative reactions are more than 100 times less
CC       efficient than the corresponding reductions, suggesting that the enzyme
CC       acts as an aldehyde reductase, rather than as an alcohol dehydrogenase.
CC       {ECO:0000269|PubMed:12423374}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC         Evidence={ECO:0000269|PubMed:12423374};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15938;
CC         Evidence={ECO:0000269|PubMed:12423374};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15939;
CC         Evidence={ECO:0000269|PubMed:12423374};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC         NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC         ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:12423374};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC         Evidence={ECO:0000269|PubMed:12423374};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methylbutanol + NADP(+) = 3-methylbutanal + H(+) + NADPH;
CC         Xref=Rhea:RHEA:18525, ChEBI:CHEBI:15378, ChEBI:CHEBI:15837,
CC         ChEBI:CHEBI:16638, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:12423374};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18527;
CC         Evidence={ECO:0000269|PubMed:12423374};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.043 mM for cinnamaldehyde {ECO:0000269|PubMed:12423374};
CC         KM=0.058 mM for veratraldehyde {ECO:0000269|PubMed:12423374};
CC         KM=0.049 mM for pentanal {ECO:0000269|PubMed:12423374};
CC         KM=0.048 mM for 3-methylbutanal {ECO:0000269|PubMed:12423374};
CC         KM=0.011 mM for NADPH {ECO:0000269|PubMed:12423374};
CC         KM=0.008 mM for cinnamyl alcohol {ECO:0000269|PubMed:12423374};
CC         KM=2.2 mM for phenylethanol {ECO:0000269|PubMed:12423374};
CC         KM=0.99 mM for pentanol {ECO:0000269|PubMed:12423374};
CC         KM=1.61 mM for 3-methylbutanol {ECO:0000269|PubMed:12423374};
CC         KM=0.013 mM for NADP {ECO:0000269|PubMed:12423374};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12423374}.
CC   -!- INTERACTION:
CC       P25377; Q12265: PRS5; NbExp=2; IntAct=EBI-2347652, EBI-9886;
CC   -!- MISCELLANEOUS: Present with 2870 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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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   AlphaFoldDB; P25377; -.
DR   SMR; P25377; -.
DR   BioGRID; 31077; 39.
DR   DIP; DIP-7661N; -.
DR   IntAct; P25377; 2.
DR   MINT; P25377; -.
DR   STRING; 4932.YCR105W; -.
DR   iPTMnet; P25377; -.
DR   PaxDb; 4932-YCR105W; -.
DR   PeptideAtlas; P25377; -.
DR   EnsemblFungi; YCR105W_mRNA; YCR105W; YCR105W.
DR   GeneID; 850469; -.
DR   KEGG; sce:YCR105W; -.
DR   AGR; SGD:S000000702; -.
DR   SGD; S000000702; ADH7.
DR   VEuPathDB; FungiDB:YCR105W; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   GeneTree; ENSGT00940000176642; -.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   InParanoid; P25377; -.
DR   OMA; AIMWARA; -.
DR   OrthoDB; 5353053at2759; -.
DR   BioCyc; YEAST:YCR105W-MONOMER; -.
DR   BioGRID-ORCS; 850469; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P25377; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25377; Protein.
DR   GO; GO:0052675; F:3-methylbutanol:NADP oxidoreductase activity; IEA:RHEA.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:SGD.
DR   GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006066; P:alcohol metabolic process; IDA:SGD.
DR   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF39; NADP-DEPENDENT ALCOHOL DEHYDROGENASE 6-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Zinc.
FT   CHAIN           1..361
FT                   /note="NADP-dependent alcohol dehydrogenase 7"
FT                   /id="PRO_0000160735"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         47
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         51
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         189
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         191
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         192
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         211
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         212
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         216
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         251
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         253
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         256
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         276
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         300
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         302
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   BINDING         349
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q04894"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
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
//