ADH7_YEAST
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-AUG-2022, entry version 171.
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 -!- 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; 38.
DR DIP; DIP-7661N; -.
DR IntAct; P25377; 2.
DR MINT; P25377; -.
DR STRING; 4932.YCR105W; -.
DR iPTMnet; P25377; -.
DR PaxDb; P25377; -.
DR PRIDE; P25377; -.
DR EnsemblFungi; YCR105W_mRNA; YCR105W; YCR105W.
DR GeneID; 850469; -.
DR KEGG; sce:YCR105W; -.
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; CMARNEW; -.
DR BioCyc; YEAST:YCR105W-MON; -.
DR PRO; PR:P25377; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25377; protein.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:SGD.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:SGD.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 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"
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"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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"
FT BINDING 188..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 276..278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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
