ID   ADH2_EMENI              Reviewed;         367 AA.
AC   P54202; Q5B6T9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   16-DEC-2008, entry version 50.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase II;
DE            Short=ADH II;
GN   Name=alcB; ORFNames=AN3741;
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=96418873; PubMed=8821658; DOI=10.1007/s002940050026;
RA   Hunter G.D., Jones I.G., Sealy-Lewis H.M.;
RT   "The cloning and sequencing of the alcB gene, coding for alcohol
RT   dehydrogenase II, in Aspergillus nidulans.";
RL   Curr. Genet. 29:122-129(1996).
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 (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z48000; CAA88034.1; -; Genomic_DNA.
DR   EMBL; AACD01000061; EAA59949.1; -; Genomic_DNA.
DR   PIR; S62746; S62746.
DR   RefSeq; XP_661345.1; -.
DR   HSSP; P39462; 1JVB.
DR   GeneID; 2873163; -.
DR   KEGG; ani:AN3741.2; -.
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   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    367       Alcohol dehydrogenase 2.
FT                                /FTId=PRO_0000160720.
FT   NP_BIND     187    193       NAD (By similarity).
FT   NP_BIND     286    288       NAD (By similarity).
FT   METAL        48     48       Zinc 1; catalytic (By similarity).
FT   METAL        74     74       Zinc 1; catalytic (By similarity).
FT   METAL       107    107       Zinc 2 (By similarity).
FT   METAL       110    110       Zinc 2 (By similarity).
FT   METAL       113    113       Zinc 2 (By similarity).
FT   METAL       121    121       Zinc 2 (By similarity).
FT   METAL       163    163       Zinc 1; catalytic (By similarity).
FT   BINDING     212    212       NAD (By similarity).
FT   BINDING     216    216       NAD (By similarity).
FT   BINDING     361    361       NAD (By similarity).
FT   CONFLICT    295    295       A -> R (in Ref. 1; CAA88034).
SQ   SEQUENCE   367 AA;  38690 MW;  0B65AC6CD0306663 CRC64;
     MAAPEIPKKQ KAVIYDNPGT VSTKVVELDV PEPGDNEVLI NLTHSGVCHS DFGIMTNTWK
     ILPFPTQPGQ VGGHEGVGKV VKLGAGAEAS GLKIGDRVGV KWISSACGQC PPCQDGADGL
     CFNQKVSGYY TPGTFQQYVL GPAQYVTPIP DGLPSAEAAP LLCAGVTVYA SLKRSKAQPG
     QWIVISGAGG GLGHLAVQIA AKGMGLRVIG VDHGSKEELV KASGAEHFVD ITKFPTGDKF
     EAISSHVKSL TTKGLGAHAV IVCTASNIAY AQSLLFLRYN GTMVCVGIPE NEPQAIASAY
     PGLFIQKHVH VTGSAVGNRN EAIETMEFAA RGVIKAHFRE EKMEALTEIF KEMEEGKLQG
     RVVLDLS
//