ADH_THEBR
ID ADH_THEBR Reviewed; 352 AA.
AC P14941;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=NADP-dependent isopropanol dehydrogenase;
DE EC=1.1.1.80;
GN Name=adh;
OS Thermoanaerobacter brockii (Thermoanaerobium brockii).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=29323;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 53556 / DSM 1457 / HTD4;
RX PubMed=2790012; DOI=10.1021/bi00442a004;
RA Peretz M., Burstein Y.;
RT "Amino acid sequence of alcohol dehydrogenase from the thermophilic
RT bacterium Thermoanaerobium brockii.";
RL Biochemistry 28:6549-6555(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 53556 / DSM 1457 / HTD4;
RA Burstein Y.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NADP AND ZINC.
RX PubMed=9836873; DOI=10.1006/jmbi.1998.1750;
RA Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F.;
RT "NADP-dependent bacterial alcohol dehydrogenases: crystal structure,
RT cofactor-binding and cofactor specificity of the ADHs of Clostridium
RT beijerinckii and Thermoanaerobacter brockii.";
RL J. Mol. Biol. 278:967-981(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 153-295 IN COMPLEX WITH ZINC,
RP FUNCTION, SUBUNIT, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=20102159; DOI=10.1021/bi901730x;
RA Goihberg E., Peretz M., Tel-Or S., Dym O., Shimon L., Frolow F.,
RA Burstein Y.;
RT "Biochemical and structural properties of chimeras constructed by exchange
RT of cofactor-binding domains in alcohol dehydrogenases from thermophilic and
RT mesophilic microorganisms.";
RL Biochemistry 49:1943-1953(2010).
CC -!- FUNCTION: Alcohol dehydrogenase with a preference for medium chain
CC secondary alcohols, such as 2-butanol and isopropanol. Has very low
CC activity with primary alcohols, such as ethanol. Under physiological
CC conditions, the enzyme reduces aldehydes and 2-ketones to produce
CC secondary alcohols. Is also active with acetaldehyde and
CC propionaldehyde. {ECO:0000269|PubMed:20102159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + propan-2-ol = acetone + H(+) + NADPH;
CC Xref=Rhea:RHEA:21792, ChEBI:CHEBI:15347, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17824, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.80;
CC Evidence={ECO:0000269|PubMed:20102159};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20102159};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20102159};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20102159,
CC ECO:0000269|PubMed:9836873}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X64841; CAA46053.1; -; Genomic_DNA.
DR PIR; A32973; A32973.
DR PDB; 1BXZ; X-ray; 2.99 A; A/B/C/D=1-352.
DR PDB; 1YKF; X-ray; 2.50 A; A/B/C/D=1-352.
DR PDB; 2NVB; X-ray; 2.80 A; A/B/C/D=1-352.
DR PDB; 3FPC; X-ray; 1.40 A; A/B/C/D=1-152, A/B/C/D=295-352.
DR PDB; 3FPL; X-ray; 1.90 A; A=153-295.
DR PDB; 3FSR; X-ray; 2.20 A; A/B/C/D=1-152, A/B/C/D=296-352.
DR PDB; 3FTN; X-ray; 2.19 A; A/B/C/D=1-152, A/B/C/D=296-352.
DR PDB; 6SDM; X-ray; 2.85 A; A/B/C/D=1-352.
DR PDB; 7F3P; X-ray; 2.60 A; A/B/C/D=1-352.
DR PDBsum; 1BXZ; -.
DR PDBsum; 1YKF; -.
DR PDBsum; 2NVB; -.
DR PDBsum; 3FPC; -.
DR PDBsum; 3FPL; -.
DR PDBsum; 3FSR; -.
DR PDBsum; 3FTN; -.
DR PDBsum; 6SDM; -.
DR PDBsum; 7F3P; -.
DR AlphaFoldDB; P14941; -.
DR SMR; P14941; -.
DR DrugBank; DB02606; 2-Butanol.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR BRENDA; 1.1.1.2; 1463.
DR BRENDA; 1.1.1.80; 1463.
DR EvolutionaryTrace; P14941; -.
DR GO; GO:0050009; F:isopropanol dehydrogenase (NADP+) 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; Direct protein sequencing; Metal-binding; NADP;
KW Oxidoreductase; Zinc.
FT CHAIN 1..352
FT /note="NADP-dependent isopropanol dehydrogenase"
FT /id="PRO_0000160749"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20102159,
FT ECO:0000269|PubMed:9836873"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20102159,
FT ECO:0000269|PubMed:9836873"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20102159,
FT ECO:0000269|PubMed:9836873"
FT BINDING 175..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:9836873"
FT BINDING 198..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:9836873"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:9836873"
FT BINDING 265..267
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:9836873"
FT BINDING 340
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:9836873"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3FPC"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:3FPC"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:7F3P"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3FPC"
FT TURN 146..150
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3FPL"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:3FPL"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3FPL"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3FPL"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:3FPL"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3FPL"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3FPL"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:3FPL"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3FPL"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:3FPL"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:3FPL"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:3FPL"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1YKF"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:3FPL"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:3FPL"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 329..338
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:3FPC"
SQ SEQUENCE 352 AA; 37647 MW; E124A5351AD55185 CRC64;
MKGFAMLSIG KVGWIEKEKP APGPFDAIVR PLAVAPCTSD IHTVFEGAIG ERHNMILGHE
AVGEVVEVGS EVKDFKPGDR VVVPAITPDW RTSEVQRGYH QHSGGMLAGW KFSNVKDGVF
GEFFHVNDAD MNLAHLPKEI PLEAAVMIPD MMTTGFHGAE LADIELGATV AVLGIGPVGL
MAVAGAKLRG AGRIIAVGSR PVCVDAAKYY GATDIVNYKD GPIESQIMNL TEGKGVDAAI
IAGGNADIMA TAVKIVKPGG TIANVNYFGE GEVLPVPRLE WGCGMAHKTI KGGLCPGGRL
RMERLIDLVF YKRVDPSKLV THVFRGFDNI EKAFMLMKDK PKDLIKPVVI LA
