ID   ADH1_BACST     STANDARD;      PRT;   337 AA.
AC   P12311;
DT   01-OCT-1989 (Rel. 12, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Alcohol dehydrogenase (EC 1.1.1.1) (ADH-T).
GN   Name=adhT;
OS   Bacillus stearothermophilus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND MUTAGENESIS.
RC   STRAIN=NCA 1503;
RX   MEDLINE=92138636; PubMed=1735726;
RA   Sakoda H., Imanaka T.;
RT   "Cloning and sequencing of the gene coding for alcohol dehydrogenase
RT   of Bacillus stearothermophilus and rational shift of the optimum pH.";
RL   J. Bacteriol. 174:1397-1402(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-45.
RX   MEDLINE=73229257; PubMed=4578954; DOI=10.1016/0014-5793(73)80144-9;
RA   Bridgen J., Kolb E., Harris J.I.;
RT   "Amino acid sequence homology in alcohol dehydrogenase.";
RL   FEBS Lett. 33:1-3(1973).
RN   [3]
RP   PROTEIN SEQUENCE OF 34-54.
RX   MEDLINE=79169263; PubMed=436831;
RA   Jeck R., Woenckhaus C., Harris J.I., Runswick M.J.;
RT   "Identification of the amino acid residue modified in Bacillus
RT   stearothermophilus alcohol dehydrogenase by the NAD+ analogue 4-(3-
RT   bromoacetylpyridinio)butyldiphosphoadenosine.";
RL   Eur. J. Biochem. 93:57-64(1979).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-37; 188-197; 247-263 AND 324-336.
RC   STRAIN=NCA 1503;
RX   MEDLINE=94325354; PubMed=8049268; DOI=10.1016/0167-4781(94)90199-6;
RA   Robinson G.A., Bailey C.J., Dowds B.C.A.;
RT   "Gene structure and amino acid sequences of alcohol dehydrogenases of
RT   Bacillus stearothermophilus.";
RL   Biochim. Biophys. Acta 1218:432-434(1994).
CC   -!- FUNCTION: Thermostable NAD(+)-dependent alcohol dehydrogenase.
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Substrate inhibition is not observed with any
CC       alcohols, and the enzyme-NADH dissociation is not considered to be
CC       a rate-limiting step.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; D90421; BAA14411.1; -.
DR   PIR; A42654; A42654.
DR   HSSP; P39462; 1JVB.
DR   InterPro; IPR002328; ADH_zinc.
DR   InterPro; IPR002085; Adh_zn_family.
DR   InterPro; IPR011032; GroES_like.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
KW   Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   METAL        38     38       Zinc 1 (catalytic) (By similarity).
FT   METAL        61     61       Zinc 1 (catalytic) (By similarity).
FT   METAL        92     92       Zinc 2 (By similarity).
FT   METAL        95     95       Zinc 2 (By similarity).
FT   METAL        98     98       Zinc 2 (By similarity).
FT   METAL       106    106       Zinc 2 (By similarity).
FT   METAL       148    148       Zinc 1 (catalytic) (By similarity).
FT   MUTAGEN      40     40       T->S: Little decrease in activity.
FT   MUTAGEN      43     43       H->R: Higher level of activity at pH 9.
FT   MUTAGEN      38     38       C->S: No activity.
FT   MUTAGEN      40     40       T->A: No activity.
FT   MUTAGEN      43     43       H->A: No activity.
FT   CONFLICT     22     22       Missing (in Ref. 2).
FT   CONFLICT     33     33       Missing (in Ref. 2).
FT   CONFLICT     52     53       KP -> PK (in Ref. 3).
SQ   SEQUENCE   337 AA;  36100 MW;  B9B35A80EE9B7A86 CRC64;
     MKAAVVEQFK KPLQVKEVEK PKISYGEVLV RIKACGVCHT DLHAAHGDWP VKPKLPLIPG
     HEGVGVIEEV GPGVTHLKVG DRVGIPWLYS ACGHCDYCLS GQETLCERQQ NAGYSVDGGY
     AEYCRAAADY VVKIPDNLSF EEAAPIFCAG VTTYKALKVT GAKPGEWVAI YGIGGLGHVA
     VQYAKAMGLN VVAVDLGDEK LELAKQLGAD LVVNPKHDDA AQWIKEKVGG VHATVVTAVS
     KAAFESAYKS IRRGGACVLV GLPPEEIPIP IFDTVLNGVK IIGSIVGTRK DLQEALQFAA
     EGKVKTIVEV QPLENINDVF DRMLKGQING RVVLKVD
//