ID   ADH1_KLUMA              Reviewed;         348 AA.
AC   Q07288;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 50.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
GN   Name=ADH1;
OS   Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=4911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12424 / NRRL Y-610;
RX   MEDLINE=93250057; PubMed=8485163;
RA   Ladriere J.-M., Delcour J., Vandenhaute J.;
RT   "Sequence of a gene coding for a cytoplasmic alcohol dehydrogenase
RT   from Kluyveromyces marxianus ATCC 12424.";
RL   Biochim. Biophys. Acta 1173:99-101(1993).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; X60224; CAA42785.1; -; Genomic_DNA.
DR   PIR; S32521; S32521.
DR   HSSP; P39462; 1JVB.
DR   SMR; Q07288; 2-348.
DR   BRENDA; 1.1.1.1; 97088.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR013149; ADH_Zn-bd.
DR   InterPro; IPR002328; ADH_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   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    348       Alcohol dehydrogenase 1.
FT                                /FTId=PRO_0000160724.
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).
SQ   SEQUENCE   348 AA;  37159 MW;  A75D2EBE82E355BD CRC64;
     MAIPETQKGV IFYEHGGELQ YKDIPVPKPK PNELLINVKY SGVCHTDLHA WQGDWPLDTK
     LPLVGGHEGA GIVVAMGENV TGWEIGDYAG IKWLNGSCMS CEECELSNEP NCPKADLSGY
     THDGSFQQYA TADAVQAARI PKNVDLAEVA PILCAGVTVY KALKSAHIKA GDWVAISGAC
     GGLGSLAIQY AKAMGYRVLG IDAGDEKAKL FKELGGEYFI DFTKTKDMVA EVIEATNGVA
     HAVINVSVSE AAISTSVLYT RSNGTVVLVG LPRDAQCKSD VFNQVVKSIS IVGSYVGNRA
     DTREALDFFS RGLVKAPIKI LGLSELASVY DKMVKGQIVG RIVVDTSK
//