ID   ADH1B_PANTR             Reviewed;         375 AA.
AC   Q5R1W2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 37.
DE   RecName: Full=Alcohol dehydrogenase 1B;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase subunit beta;
GN   Name=ADH1B;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RA   Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y.,
RA   Osada N., Hashimoto K.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer or heterodimer of closely related subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; AB188285; BAD74036.1; -; mRNA.
DR   RefSeq; NP_001029330.1; -.
DR   SMR; Q5R1W2; 1-374, 2-375.
DR   Ensembl; ENSPTRG00000023494; Pan troglodytes.
DR   GeneID; 461396; -.
DR   KEGG; ptr:461396; -.
DR   HOVERGEN; Q5R1W2; -.
DR   OMA; Q5R1W2; LEPLITH.
DR   BRENDA; 1.1.1.1; 264977.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    375       Alcohol dehydrogenase 1B.
FT                                /FTId=PRO_0000160662.
FT   NP_BIND     200    205       NAD (By similarity).
FT   NP_BIND     293    295       NAD (By similarity).
FT   METAL        47     47       Zinc 1; catalytic (By similarity).
FT   METAL        68     68       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       175    175       Zinc 1; catalytic (By similarity).
FT   BINDING     224    224       NAD (By similarity).
FT   BINDING     229    229       NAD (By similarity).
FT   BINDING     370    370       NAD (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
SQ   SEQUENCE   375 AA;  39826 MW;  5CE9BC266A776F25 CRC64;
     MSTAGKVIKC KAAVLWEVKK PFSIEDVEVA PPKAYEVRIK MVAVGICRTD DHVVSGNLVT
     PLPAILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRVCKNPESN YCLKNDLGNP
     RGTLQDGTRR FTCRGKPIHH FLGTSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
     YGSAVNVAKV TPGSTCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE
     CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPASQ
     NLSINPMLLL TGRTWKGAVY GGFKSKEGIP KLVADFMAKK FSLDALITHV LPFEKINEGF
     DLLHSGKSIR TVLTF
//