ID   ADH3_EMENI              Reviewed;         352 AA.
AC   P07754; Q5BAZ4;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=Alcohol dehydrogenase 3;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase III;
DE            Short=ADH III;
GN   Name=alcC; Synonyms=adh3; ORFNames=AN2286;
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.
OX   NCBI_TaxID=162425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86055769; PubMed=2998782;
RA   McKnight L., Kato H., Upshall A., Parker M.D., O'Hara P.J., O'Hara S.;
RT   "Identification and molecular analysis of a third Aspergillus nidulans
RT   alcohol dehydrogenase gene.";
RL   EMBO J. 4:2093-2099(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC 4;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; X02764; CAA26541.1; -; Genomic_DNA.
DR   EMBL; AACD01000038; EAA64397.1; -; Genomic_DNA.
DR   PIR; A24648; A24648.
DR   RefSeq; XP_659890.1; -.
DR   HSSP; P39462; 1JVB.
DR   GeneID; 2874791; -.
DR   KEGG; ani:AN2286.2; -.
DR   BRENDA; 1.1.1.1; 3859.
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    352       Alcohol dehydrogenase 3.
FT                                /FTId=PRO_0000160721.
FT   NP_BIND     180    186       NAD (By similarity).
FT   NP_BIND     273    275       NAD (By similarity).
FT   METAL        44     44       Zinc 1; catalytic (By similarity).
FT   METAL        67     67       Zinc 1; catalytic (By similarity).
FT   METAL       100    100       Zinc 2 (By similarity).
FT   METAL       103    103       Zinc 2 (By similarity).
FT   METAL       106    106       Zinc 2 (By similarity).
FT   METAL       114    114       Zinc 2 (By similarity).
FT   METAL       156    156       Zinc 1; catalytic (By similarity).
FT   BINDING     204    204       NAD (By similarity).
FT   BINDING     209    209       NAD (By similarity).
FT   BINDING     345    345       NAD (By similarity).
SQ   SEQUENCE   352 AA;  37126 MW;  AFDE78FE442E3144 CRC64;
     MSVPEVQWAQ VVEKAGTPPV YKQVPVPKPG PDEILVKMRY SGVCHTDLHA MKGDWPLPSK
     MPLIGGHEGA GVVVAKGELV KDEDFKIGDR AGIKWLNGSC LSCEMCMQAD EPLCPHASLS
     GYTVDGTFQQ YTIGKAALAS KIPDNVPLDA AAPILCAGIT VYKGLKESGA RPGQTVAIVG
     AGGGLGSLAQ QYAKAMGLRT IAIDSGDEKK AMCEQLGAEV FIDFSKSADV VADVKAATPG
     GLGAHAVILL AVAEKPFQQA TEYVRSHGSV VAIGLPANAF LKAPVFTTVV RMINIKGSYV
     GNRQDGVEAL DFFARGLIKA PFKKAPLQDL PQIFELMGQG KIAGRYVLEI PE
//