ADH_THEBA
ID ADH_THEBA Reviewed; 378 AA.
AC A0A0S1X9S7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Alcohol dehydrogenase {ECO:0000303|PubMed:33428959};
DE EC=1.1.1.1 {ECO:0000269|PubMed:33428959};
GN ORFNames=TBCH5v1_0547 {ECO:0000312|EMBL:ALM74514.1};
OS Thermococcus barophilus.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=55802;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ch5;
RX PubMed=26769929; DOI=10.1128/genomea.01534-15;
RA Oger P., Sokolova T.G., Kozhevnikova D.A., Taranov E.A., Vannier P.,
RA Lee H.S., Kwon K.K., Kang S.G., Lee J.H., Bonch-Osmolovskaya E.A.,
RA Lebedinsky A.V.;
RT "Complete genome sequence of the hyperthermophilic and piezophilic archaeon
RT Thermococcus barophilus Ch5, capable of growth at the expense of
RT hydrogenogenesis from carbon monoxide and formate.";
RL Genome Announc. 4:0-0(2016).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-195; HIS-199; HIS-262; HIS-266 AND HIS-274.
RC STRAIN=Ch5;
RX PubMed=33428959; DOI=10.1016/j.ijbiomac.2020.12.197;
RA Zhang L., Jiang D., Li Y., Wu L., Liu Q., Dong K., Oger P.;
RT "Characterization of a novel type III alcohol dehydrogenase from
RT Thermococcus barophilus Ch5.";
RL Int. J. Biol. Macromol. 171:491-501(2021).
CC -!- FUNCTION: Thermostable type III alcohol dehydrogenase. For oxidation
CC activity, the best substrates are 1-butanol and 1-hexanol, followed by
CC ethanol. Shows lower activity with ethylene glycol, isopentanol,
CC isopropanol and glycerol. Displays higher reduction activity in the
CC presence of butanal, followed by acetaldehyde. Has lower activity with
CC hexanal and acetone. {ECO:0000269|PubMed:33428959}.
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 Evidence={ECO:0000269|PubMed:33428959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butan-1-ol + NAD(+) = butanal + H(+) + NADH;
CC Xref=Rhea:RHEA:33199, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:33428959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexan-1-ol + NAD(+) = H(+) + hexanal + NADH;
CC Xref=Rhea:RHEA:60972, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:87393, ChEBI:CHEBI:88528;
CC Evidence={ECO:0000269|PubMed:33428959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:33428959};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:33428959};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:33428959};
CC Note=Dependent on a divalent cation for ethanol oxidation, among which
CC Mn(2+) is optimal. Compared with the oxidation reaction, displays about
CC 30% acetaldehyde reduction in the absence of divalent cation. Shows
CC maximal reduction activity in the presence of Fe(2+).
CC {ECO:0000269|PubMed:33428959};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=92 mM for ethanol {ECO:0000269|PubMed:33428959};
CC KM=34.5 mM for acetaldehyde {ECO:0000269|PubMed:33428959};
CC Note=kcat is 0.27 sec(-1) for ethanol oxidation. kcat is 69 sec(-1)
CC for acetaldehyde reduction. {ECO:0000269|PubMed:33428959};
CC pH dependence:
CC Optimum pH is 8.5 for oxidation and 7.0 for reduction.
CC {ECO:0000269|PubMed:33428959};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius for both ethanol oxidation
CC and acetaldehyde reduction. {ECO:0000269|PubMed:33428959};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CP013050; ALM74514.1; -; Genomic_DNA.
DR RefSeq; WP_056933392.1; NZ_CP013050.1.
DR SMR; A0A0S1X9S7; -.
DR STRING; 55802.TBCH5v1_0547; -.
DR EnsemblBacteria; ALM74514; ALM74514; TBCH5v1_0547.
DR GeneID; 26135831; -.
DR PATRIC; fig|55802.8.peg.544; -.
DR Proteomes; UP000066042; Chromosome.
DR GO; GO:1990362; F:butanol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08179; NADPH_BDH; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR034802; NADPH_BDH.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
PE 1: Evidence at protein level;
KW Iron; Manganese; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..378
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000453259"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 274
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT MUTAGEN 195
FT /note="D->A: Disrupts the overall structure of the enzyme.
FT Lack of acetaldehyde reduction activity and displays weak
FT ethanol oxidation activity."
FT /evidence="ECO:0000269|PubMed:33428959"
FT MUTAGEN 199
FT /note="H->A: Disrupts the overall structure of the enzyme.
FT Retains 10% of ethanol oxidation and acetaldehyde reduction
FT activities."
FT /evidence="ECO:0000269|PubMed:33428959"
FT MUTAGEN 262
FT /note="H->A: Disrupts the overall structure of the enzyme.
FT Displays weak ethanol oxidation and acetaldehyde reduction
FT activities."
FT /evidence="ECO:0000269|PubMed:33428959"
FT MUTAGEN 266
FT /note="H->A: Disrupts the overall structure of the enzyme.
FT Displays higher acetaldehyde reduction activity (134%) but
FT lower ethanol oxidation activity (36%)."
FT /evidence="ECO:0000269|PubMed:33428959"
FT MUTAGEN 274
FT /note="H->A: Disrupts the overall structure of the enzyme.
FT Retains 20% of ethanol oxidation and acetaldehyde reduction
FT activities."
FT /evidence="ECO:0000269|PubMed:33428959"
SQ SEQUENCE 378 AA; 42248 MW; 52C79F1301456889 CRC64;
MQFFSLKTRI VLGEGSLSYI KSVAKKHSRV LIFSSKSMRV HGFLNETMNY VEDANAEVEA
ITGVPAEPSY EYVESIMPKV REFQPDLIVA LGGGSVIDVA KAVKVFYDAP ELKFEEVAFI
SRFEKPKPIP KLKTPLIAIP STSGAGSEVS AASVLKKGDI KYNLVSFEIA PEFAILDPRL
PRTMPKEVAR NSGLDVLVHG IEAYTTTAAT PFSDAMAIKA IKLVYKWLPL SVQGDEKARE
NVHYAATMAG IAFLNARLGL CHSLSHKAAW IAPHGLLNAI FLPYVMEFNM RSEYARKRYA
EIARELGFNT AQELIEVIRE FNEMLGVPKL SELVSEEEFL SKLDEMSEKA YHDPLINFNP
VEPSIEEIKE LYKRAFYD
