ADH3_GEOSE
ID ADH3_GEOSE Reviewed; 339 AA.
AC P42328;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
DE AltName: Full=ADH-HT;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 12403 / LLD-R;
RX PubMed=8020473; DOI=10.1111/j.1432-1033.1994.tb18873.x;
RA Cannio R., Rossi M., Bartolucci S.;
RT "A few amino acid substitutions are responsible for the higher
RT thermostability of a novel NAD(+)-dependent bacillar alcohol
RT dehydrogenase.";
RL Eur. J. Biochem. 222:345-352(1994).
CC -!- FUNCTION: Thermophilic NAD(+)-dependent alcohol dehydrogenase. Bears
CC mainly an ethanol-dehydrogenase activity.
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 -!- 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; Z27089; CAA81612.1; -; Genomic_DNA.
DR PIR; S45605; S45605.
DR PDB; 1RJW; X-ray; 2.35 A; A/B/C/D=1-339.
DR PDB; 3PII; X-ray; 2.90 A; A/B/C/D=1-339.
DR PDBsum; 1RJW; -.
DR PDBsum; 3PII; -.
DR AlphaFoldDB; P42328; -.
DR SMR; P42328; -.
DR DrugBank; DB03226; Trifluoroethanol.
DR BRENDA; 1.1.1.1; 623.
DR EvolutionaryTrace; P42328; -.
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 3D-structure; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..339
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000160738"
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 STRAND 2..8
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3PII"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1RJW"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1RJW"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1RJW"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:1RJW"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1RJW"
SQ SEQUENCE 339 AA; 36338 MW; AED17E4A34163430 CRC64;
MKAAVVEQFK EPLKIKEVEK PTISYGEVLV RIKACGVCHT DLHAAHGDWP VKPKLPLIPG
HEGVGIVEEV GPGVTHLKVG DRVGIPWLYS ACGHCDYCLS GQETLCEHQK NAGYSVDGGY
AEYCRAAADY VVKIPDNLSF EEAAPIFCAG VTTYKALKVT GAKPGEWVAI YGIGGLGHVA
VQYAKAMGLN VVAVDIGDEK LELAKELGAD LVVNPLKEDA AKFMKEKVGG VHAAVVTAVS
KPAFQSAYNS IRRGGACVLV GLPPEEMPIP IFDTVLNGIK IIGSIVGTRK DLQEALQFAA
EGKVKTIIEV QPLEKINEVF DRMLKGQING RVVLTLEDK
