ADH1_ENTHI
ID ADH1_ENTHI Reviewed; 360 AA.
AC P35630;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=NADP-dependent isopropanol dehydrogenase;
DE EC=1.1.1.80;
GN Name=ADH1;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1438208; DOI=10.1073/pnas.89.21.10188;
RA Kumar A., Shen P.S., Descoteaux S., Pohl J., Bailey G., Samuelson J.;
RT "Cloning and expression of an NADP(+)-dependent alcohol dehydrogenase gene
RT of Entamoeba histolytica.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10188-10192(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1340318;
RA Samuelson J., Zhang W.W., Kumar A., Descoteaux S., Shen P.S., Bailey G.;
RT "Primary structures of alcohol and aldehyde dehydrogenase genes of
RT Entamoeba histolytica.";
RL Arch. Med. Res. 23:31-33(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
RP SUBUNIT.
RX PubMed=16627948; DOI=10.1107/s0907444906009292;
RA Shimon L.J.W., Goihberg E., Peretz M., Burstein Y., Frolow F.;
RT "Structure of alcohol dehydrogenase from Entamoeba histolytica.";
RL Acta Crystallogr. D 62:541-547(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RX PubMed=18260103; DOI=10.1002/prot.21946;
RA Goihberg E., Dym O., Tel-Or S., Shimon L., Frolow F., Peretz M.,
RA Burstein Y.;
RT "Thermal stabilization of the protozoan Entamoeba histolytica alcohol
RT dehydrogenase by a single proline substitution.";
RL Proteins 72:711-719(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR,
RP FUNCTION, SUBUNIT, 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: Homodimer. {ECO:0000269|PubMed:16627948,
CC ECO:0000269|PubMed:18260103, ECO:0000269|PubMed:20102159}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M88600; AAA51479.1; -; mRNA.
DR PIR; A46409; A46409.
DR PDB; 1Y9A; X-ray; 1.81 A; A/C=1-360.
DR PDB; 2OUI; X-ray; 1.77 A; A/B/C/D=1-360.
DR PDB; 3FPC; X-ray; 1.40 A; A/B/C/D=153-294.
DR PDBsum; 1Y9A; -.
DR PDBsum; 2OUI; -.
DR PDBsum; 3FPC; -.
DR AlphaFoldDB; P35630; -.
DR SMR; P35630; -.
DR STRING; 5759.rna_EHI_023110-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_147830; -.
DR VEuPathDB; AmoebaDB:EHI7A_198240; -.
DR VEuPathDB; AmoebaDB:EHI8A_215180; -.
DR VEuPathDB; AmoebaDB:EHI_023110; -.
DR VEuPathDB; AmoebaDB:KM1_205210; -.
DR eggNOG; KOG0024; Eukaryota.
DR BRENDA; 1.1.1.2; 2080.
DR EvolutionaryTrace; P35630; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Cytoplasm; Direct protein sequencing; Metal-binding; NADP;
KW Oxidoreductase; Zinc.
FT CHAIN 1..360
FT /note="NADP-dependent isopropanol dehydrogenase"
FT /id="PRO_0000160695"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20102159"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20102159"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20102159"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:20102159"
FT BINDING 175..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 198..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 265..267
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2OUI"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:2OUI"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:3FPC"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:3FPC"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:3FPC"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:3FPC"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3FPC"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:2OUI"
FT HELIX 329..339
FT /evidence="ECO:0007829|PDB:2OUI"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:2OUI"
FT TURN 354..358
FT /evidence="ECO:0007829|PDB:2OUI"
SQ SEQUENCE 360 AA; 38568 MW; 6D01643EB4A3A07F CRC64;
MKGLAMLGIG RIGWIEKKIP ECGPLDALVR PLALAPCTSD THTVWAGAIG DRHDMILGHE
AVGQIVKVGS LVKRLKVGDK VIVPAITPDW GEEESQRGYP MHSGGMLGGW KFSNFKDGVF
SEVFHVNEAD ANLALLPRDI KPEDAVMLSD MVTTGFHGAE LANIKLGDTV CVIGIGPVGL
MSVAGANHLG AGRIFAVGSR KHCCDIALEY GATDIINYKN GDIVEQILKA TDGKGVDKVV
IAGGDVHTFA QAVKMIKPGS DIGNVNYLGE GDNIDIPRSE WGVGMGHKHI HGGLTPGGRV
RMEKLASLIS TGKLDTSKLI THRFEGLEKV EDALMLMKNK PADLIKPVVR IHYDDEDTLH
