ID   ADH2_KLULA              Reviewed;         348 AA.
AC   P49383; Q6CJJ0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   16-DEC-2008, entry version 57.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase II;
GN   Name=ADH2; OrderedLocusNames=KLLA0F18260g;
OS   Kluyveromyces lactis (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=28985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   MEDLINE=92269769; PubMed=1588917; DOI=10.1007/BF00266253;
RA   Shain D.H., Salvadore C., Denis C.L.;
RT   "Evolution of the alcohol dehydrogenase (ADH) genes in yeast:
RT   characterization of a fourth ADH in Kluyveromyces lactis.";
RL   Mol. Gen. Genet. 232:479-488(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; X64397; CAA45739.1; -; Genomic_DNA.
DR   EMBL; CR382126; CAG98607.1; -; Genomic_DNA.
DR   PIR; S20911; S20911.
DR   RefSeq; XP_455899.1; -.
DR   HSSP; P39462; 1JVB.
DR   SMR; P49383; 2-348.
DR   GeneID; 2894942; -.
DR   KEGG; kla:KLLA0F18260g; -.
DR   HOGENOM; P49383; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Zinc.
FT   CHAIN         1    348       Alcohol dehydrogenase 2.
FT                                /FTId=PRO_0000160723.
FT   NP_BIND     178    184       NAD (By similarity).
FT   NP_BIND     269    271       NAD (By similarity).
FT   METAL        44     44       Zinc 1; catalytic (By similarity).
FT   METAL        67     67       Zinc 1; catalytic (By similarity).
FT   METAL        98     98       Zinc 2 (By similarity).
FT   METAL       101    101       Zinc 2 (By similarity).
FT   METAL       104    104       Zinc 2 (By similarity).
FT   METAL       112    112       Zinc 2 (By similarity).
FT   METAL       154    154       Zinc 1; catalytic (By similarity).
FT   BINDING     202    202       NAD (By similarity).
FT   BINDING     207    207       NAD (By similarity).
FT   BINDING     341    341       NAD (By similarity).
FT   CONFLICT     84     84       N -> I (in Ref. 1; CAA45739).
SQ   SEQUENCE   348 AA;  37098 MW;  F21D3DE1F6FB389C CRC64;
     MSIPETQKGV IFYENGGELQ YKDIPVPKPK ANELLINVKY SGVCHTDLHA WKGDWPLPTK
     LPLVGGHEGA GVVVAMGENV KGWNIGDFAG IKWLNGSCMS CEYCELSNES NCPDADLSGY
     THDGSFQQYA TADAVQAARI PKGTDLAEVA PILCAGVTVY KALKSADLKA GDWVAISGAC
     GGLGSLAIQY AKAMGYRVLG IDTGAEKAKL FKELGGEYFV DYAVSKDLIK EIVDATNGGA
     HGVINVSVSE FAIEQSTNYV RSNGTVVLVG LPRDAKCKSD VFTQVVKSVS IVGSYVGNRA
     DTREALDFFA RGLVHAPIKI VGLSELADVY DKMVKGEIVG RYVVDTSK
//