ID   ADH1_APTAU              Reviewed;         375 AA.
AC   P49645;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 52.
DE   RecName: Full=Alcohol dehydrogenase 1;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase I;
GN   Name=ADH1;
OS   Apteryx australis (Brown kiwi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Palaeognathae; Apterygiformes; Apterygidae; Apteryx.
OX   NCBI_TaxID=8822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=95331397; PubMed=7541757; DOI=10.1016/0014-5793(95)00554-M;
RA   Hjelmqvist L., Metsis M., Persson H., Hoeoeg J.-O., McLennan J.,
RA   Joernvall H.;
RT   "Alcohol dehydrogenase of class I: kiwi liver enzyme, parallel
RT   evolution in separate vertebrate lines, and correlation with 12S rRNA
RT   patterns.";
RL   FEBS Lett. 367:306-310(1995).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-2.
RX   PubMed=7607314; DOI=10.1016/0014-5793(95)00572-Q;
RA   Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J.,
RA   Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Jornvall H.;
RT   "Multiplicity of N-terminal structures of medium-chain alcohol
RT   dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate
RT   and higher vertebrate class I, II, and III forms of the enzyme.";
RL   FEBS Lett. 367:237-240(1995).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-I subfamily.
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DR   EMBL; S78778; AAC60755.2; -; mRNA.
DR   PIR; S66272; S66272.
DR   HSSP; P00326; 1HT0.
DR   SMR; P49645; 2-375.
DR   HOVERGEN; P49645; -.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD;
KW   Oxidoreductase; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    375       Alcohol dehydrogenase 1.
FT                                /FTId=PRO_0000160671.
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   MOD_RES       2      2       N-acetylserine.
SQ   SEQUENCE   375 AA;  39631 MW;  A6EBC1BEB0D66E02 CRC64;
     MSTAGKVIKC KAAVLWEPKK PFSIEEVEVA PPKAHEVRIK ILATGICRSD DHVITGALVR
     PFPIILGHEA AGVVESVGEG VTSVKPGDKV IPLFVPQCGE CSACLSTKGN LCSKNDIGSA
     SGLMPDGTTR FTCKGKAIHH FIGTSTFTEY TVVHETAVAK IAAAAPLEKV CLIGCGFSTG
     YGAAVQTAKV EPGSTCAVFG LGGVGLSVVM GCKAAGASRI IAIDINKDKF AKAKELGATD
     CVNPKDFTKP IHEVLMEMTG LGVDYSFEVI GHTETMAAAL ASCHFNYGVS VILGVPPAAE
     KISFDPMLLF SGRTWKGSVF GGWKSKDAVP KLVADYMEKK FVLEPLITHT LPFIKINEGF
     DLLRKGKSIR SVLVF
//