ID   ADH1_ASPFL              Reviewed;         349 AA.
AC   P41747;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-NOV-2008, entry version 47.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase I;
GN   Name=adh1;
OS   Aspergillus flavus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae;
OC   mitosporic Trichocomaceae; Aspergillus.
OX   NCBI_TaxID=5059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=NRRL 3357 / SRRC 167 / IAM 13836 / JCM 12722;
RX   MEDLINE=94182922; PubMed=8135521;
RA   Woloshuk C.P., Payne G.A.;
RT   "The alcohol dehydrogenase gene adh1 is induced in Aspergillus flavus
RT   grown on medium conducive to aflatoxin biosynthesis.";
RL   Appl. Environ. Microbiol. 60:670-676(1994).
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.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; L27434; AAA32684.1; -; mRNA.
DR   EMBL; L27433; AAA32683.1; -; Genomic_DNA.
DR   HSSP; P39462; 1JVB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    349       Alcohol dehydrogenase 1.
FT                                /FTId=PRO_0000160716.
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).
SQ   SEQUENCE   349 AA;  36901 MW;  F917FA2A03914E2F CRC64;
     MSIPEMQWAQ VAEQKGGPLI YKQIPVPKPG PDEILVKVRY SGVCHTDLHA LKGDWPLPVK
     MPLVGGHEGA GVVVARGDLV TEFEIGDHAG LKWLNGSCLA CEFCKQADEP LCPNASLSGY
     TVDGTFQQYA IGKATHASKL PKNVPLDAVA PVLCAGITVY KGLKESGVRP GQTVAIVGAG
     GGLGSLALQY AKAMGIRVVA IDGGEEKQAM CEQLGAEAYV DFTKTQDLVA DVKAATPEGL
     GAHAVILLAV AEKPFQQAAE YVSRGTVVAI GLPAGAFLRA PVFNTVVRMI NIKGSYVGNR
     QDGVEAVDFF ARGLIKAPFK TAPLQDLPKI FELMEQGKIA GRYVLEIPE
//