ID ADH2_GEOSE Reviewed; 339 AA.
AC P42327;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-MAY-2023, entry version 105.
DE RecName: Full=Alcohol dehydrogenase;
DE Short=ADH;
DE EC=1.1.1.1;
GN Name=adh;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-40.
RC STRAIN=DSM 2334 / Var. Non-diastaticus;
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: Active with primary alcohols, including methanol.
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: The rate-limiting step is NADH release. Catabolite
CC repression.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z25544; CAA80989.1; -; Genomic_DNA.
DR PIR; S47643; S47643.
DR PDB; 6IQD; X-ray; 2.84 A; A/B/C/D/E/F/G/H=1-339.
DR PDBsum; 6IQD; -.
DR AlphaFoldDB; P42327; -.
DR SMR; P42327; -.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Zinc.
FT CHAIN 1..339
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000160737"
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..6
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6IQD"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:6IQD"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6IQD"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6IQD"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:6IQD"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:6IQD"
SQ SEQUENCE 339 AA; 36205 MW; 0EC33CE7287D7476 CRC64;
MKAAVVNEFK KALEIKEVER PKLEEGEVLV KIEACGVCHT DLHAAHGDWP IKPKLPLIPG
HEGVGIVVEV AKGVKSIKVG DRVGIPWLYS ACGECEYCLT GQETLCPHQL NGGYSVDGGY
AEYCKAPADY VAKIPDNLDP VEVAPILCAG VTTYKALKVS GARPGEWVAI YGIGGLGHIA
LQYAKAMGLN VVAVDISDEK SKLAKDLGAD IAINGLKEDP VKAIHDQVGG VHAAISVAVN
KKAFEQAYQS VKRGGTLVVV GLPNADLPIP IFDTVLNGVS VKGSIVGTRK DMQEALDFAA
RGKVRPIVET AELEEINEVF ERMEKGKING RIVLKLKED
//
