ID   ADH1A_UROHA             Reviewed;         375 AA.
AC   P25405;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   02-SEP-2008, entry version 53.
DE   RecName: Full=Alcohol dehydrogenase 1A;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase I-A;
DE            Short=ADH IA;
OS   Uromastyx hardwickii (Indian spiny-tailed lizard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Iguania; Acrodonta; Agamidae; Uromastycinae;
OC   Uromastyx.
OX   NCBI_TaxID=40250;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=96195666; PubMed=8612630;
RA   Hjelmqvist L., Shafqat J., Siddiqi A.R., Joernvall H.;
RT   "Linking of isozyme and class variability patterns in the emergence of
RT   novel alcohol dehydrogenase functions. Characterization of isozymes in
RT   Uromastix hardwickii.";
RL   Eur. J. Biochem. 236:563-570(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-18.
RC   TISSUE=Liver;
RX   MEDLINE=92183888; PubMed=1544464; DOI=10.1016/0014-5793(92)80080-Z;
RA   Hjelmqvist L., Ericsson M., Shafqat J., Carlquist M., Siddiqi A.R.,
RA   Hoeoeg J.-O., Joernvall H.;
RT   "Reptilian alcohol dehydrogenase. Heterogeneity relevant to class
RT   multiplicity of the mammalian enzyme.";
RL   FEBS Lett. 298:297-300(1992).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Multimeric (with different ratios of monomers).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: In U.hardwickii there are two isozymes of alcohol
CC       dehydrogenase I.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-I subfamily.
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DR   PIR; S62638; S62638.
DR   HSSP; P00328; 1EE2.
DR   SMR; P25405; 2-375.
DR   HOVERGEN; P25405; -.
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   CHAIN         1    375       Alcohol dehydrogenase 1A.
FT                                /FTId=PRO_0000160677.
FT   METAL        46     46       Zinc 1; catalytic (By similarity).
FT   METAL        67     67       Zinc 1; catalytic (By similarity).
FT   METAL        97     97       Zinc 2 (By similarity).
FT   METAL       100    100       Zinc 2 (By similarity).
FT   METAL       103    103       Zinc 2 (By similarity).
FT   METAL       111    111       Zinc 2 (By similarity).
FT   METAL       174    174       Zinc 1; catalytic (By similarity).
FT   MOD_RES       1      1       N-acetylglycine.
SQ   SEQUENCE   375 AA;  39663 MW;  F315BB777996D906 CRC64;
     GTAGKVIKCK AAIAWEIKKP LSIEQIEVAP PKAHEVRIKI LATGICRSDD HVISGAFKMP
     LPMVLGHEAA GVVESVGEGV TCVKPGDKVI PLFVPQCGKC SSCRSTRGNL CTSNDLSAAT
     GLMPDGTSRF TCKGKSLHHF ISTSSFTEYT VVHENSVVKI DAAAPLEKVC LIGCGFSTGY
     GAAVETAKVE PGSTCAVFGL GGVGLSAVMG CKAAGASRII GVDINKDKFP KAKEMGATEC
     VNPLDYKKPI NEVLFDLTGG EGVDYSFEVI GRTDTMTAAL ASCHMDYGTS IIVGLPPSAS
     EITFSPGLIF TGRTWKGSVF GGWKSKDSVP RLVSDFMQKK FSLDPLITHT MPFDKINEGF
     ELLRAGKSIR SVLLF
//