ID   ADH1G_PAPHA             Reviewed;         375 AA.
AC   O97959;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Alcohol dehydrogenase 1C;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase subunit gamma;
GN   Name=ADH1C; Synonyms=ADH3;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=99261634; PubMed=10331249;
RA   Cheung B., Holmes R.S., Easteal S., Beacham I.R.;
RT   "Evolution of class I alcohol dehydrogenase genes in catarrhine
RT   primates: gene conversion, substitution rates, and gene regulation.";
RL   Mol. Biol. Evol. 16:23-36(1999).
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   -!- TISSUE SPECIFICITY: Expressed in kidney.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; L30113; AAD09950.1; -; mRNA.
DR   HSSP; P00326; 1HT0.
DR   SMR; O97959; 1-374, 2-375.
DR   HOVERGEN; O97959; -.
DR   BRENDA; 1.1.1.1; 39388.
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 1C.
FT                                /FTId=PRO_0000160665.
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;  39841 MW;  BBB215BCD5FDB9EA CRC64;
     MSTAGKVIKC KAAVLWEVKK PFSIEEVEVA PPKAHEVRIK MVAVGICRSD DHVVSGTLVT
     PLPAILGHEA AGIVEGVGEG VTTVKPGDKV IPLFTPQCGK CRVCKNPESN YCFKNDLSNP
     RGTMQDGTRR FTCGGKPIHH FLGISTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG
     YGPAVKVAKV TPGSTCAVFG LGGVGLSAVM GCKAAGAARI IAVDINKDKF AKAKELGATE
     CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTIMASL LCCHEACGTS VIVGVPPDSQ
     NLSINPVLLL TGRTWKGAIF GGFKSKESVP KLVSDFMAKK FSLDALITNV LPFEKINEGF
     DLLRSGKSIR TILMF
//