ID   ADH2_CANAL              Reviewed;         348 AA.
AC   O94038; Q5A749;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
GN   Name=ADH2; ORFNames=Ca41C10.04, CaO19.5113, CaO19.12579;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1161;
RA   Taylor K., Harris D., Barrell B.G., Rajandream M.A.;
RT   "Candida albicans strain 1161 genome pilot sequencing project.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(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 (Probable).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; AL033501; CAA21988.1; -; Genomic_DNA.
DR   EMBL; AACQ01000053; EAK98611.1; -; Genomic_DNA.
DR   EMBL; AACQ01000052; EAK98687.1; -; Genomic_DNA.
DR   PIR; T18230; T18230.
DR   RefSeq; XP_717575.1; -.
DR   RefSeq; XP_717649.1; -.
DR   HSSP; P39462; 1JVB.
DR   SMR; O94038; 2-348.
DR   GeneID; 3640751; -.
DR   GeneID; 3640833; -.
DR   CGD; CAL0002509; ADH2.
DR   OMA; O94038; TEGGPHG.
DR   BRENDA; 1.1.1.1; 1124.
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 2.
FT                                /FTId=PRO_0000160718.
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;  36807 MW;  3D6E67538522ADCF CRC64;
     MSVPTTQKAV IFETNGGKLE YKDIPVPKPK ANELLINVKY SGVCHTDLHA WKGDWPLATK
     LPLVGGHEGA GVVVALGENV KGWKVGDYAG VKWLNGSCLN CEYCQSGAEP NCAEADLSGY
     THDGSFQQYA TADAVQAARI PAGTDLANVA PILCAGVTVY KALKTAELEA GQWVAISGAA
     GGLGSLAVQY AKAMGYRVLA IDGGEDKGEF VKSLGAETFI DFTKEKDVVE AVKKATNGGP
     HGVINVSVSE RAIGQSTEYV RTLGKVVLVG LPAGAKISTP VFDAVIKTIQ IKGSYVGNRK
     DTAEAVDFFT RGLIKCPIKI VGLSELPEVY KLMEEGKILG RYVLDNDK
//