ADH1_GEOSE
ID ADH1_GEOSE Reviewed; 337 AA.
AC P12311;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
DE AltName: Full=ADH-T;
GN Name=adhT;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=1735726; DOI=10.1128/jb.174.4.1397-1402.1992;
RA Sakoda H., Imanaka T.;
RT "Cloning and sequencing of the gene coding for alcohol dehydrogenase of
RT 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 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 PubMed=436831; DOI=10.1111/j.1432-1033.1979.tb12794.x;
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=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX 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: NAD(+)-dependent alcohol dehydrogenase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Substrate inhibition is not observed with any
CC alcohols, and the enzyme-NADH dissociation is not considered to be a
CC rate-limiting step.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; D90421; BAA14411.1; -; Genomic_DNA.
DR PIR; A42654; A42654.
DR RefSeq; WP_033015595.1; NZ_RCTH01000031.1.
DR AlphaFoldDB; P12311; -.
DR SMR; P12311; -.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..337
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000160736"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 172..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 260..262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MUTAGEN 38
FT /note="C->S: No activity."
FT /evidence="ECO:0000269|PubMed:1735726"
FT MUTAGEN 40
FT /note="T->A: No activity."
FT /evidence="ECO:0000269|PubMed:1735726"
FT MUTAGEN 40
FT /note="T->S: Little decrease in activity."
FT /evidence="ECO:0000269|PubMed:1735726"
FT MUTAGEN 43
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:1735726"
FT MUTAGEN 43
FT /note="H->R: Higher level of activity at pH 9."
FT /evidence="ECO:0000269|PubMed:1735726"
FT CONFLICT 22
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="KP -> PK (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
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
