EUTG_ECOLI
ID EUTG_ECOLI Reviewed; 395 AA.
AC P76553; P76969;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable alcohol dehydrogenase EutG {ECO:0000303|PubMed:22731523};
DE EC=1.1.1.1 {ECO:0000305|PubMed:22731523};
DE AltName: Full=Ethanolamine utilization protein EutG;
GN Name=eutG; Synonyms=yffV; OrderedLocusNames=b2453, JW2437;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND COFACTOR.
RC STRAIN=K12 / BW25113;
RX PubMed=22731523; DOI=10.1186/1475-2859-11-90;
RA Rodriguez G.M., Atsumi S.;
RT "Isobutyraldehyde production from Escherichia coli by removing aldehyde
RT reductase activity.";
RL Microb. Cell Fact. 11:90-90(2012).
CC -!- FUNCTION: May act on the acetaldehyde produced from the degradation of
CC ethanolamine, producing ethanol (By similarity). Active on acetaldehyde
CC and isobutyraldehyde in vitro. In vitro works equally well with NADH or
CC NADPH (PubMed:22731523). {ECO:0000250|UniProtKB:P41795,
CC ECO:0000269|PubMed:22731523}.
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:0000305|PubMed:22731523};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P0A9S1};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:P0A9S1}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- CAUTION: In strain MG1655 the eut operon is interrupted by the CPZ-55
CC prophage, encoding 9 genes situated between eutA and eutB, which are
CC translated in the other direction. CPZ-55 may prevent expression of the
CC eut operon in strain MG1655. Strain W3110 does not have this prophage
CC element and should be able to express the operon.
CC {ECO:0000305|PubMed:9278503}.
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DR EMBL; U00096; AAC75506.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16331.1; -; Genomic_DNA.
DR PIR; D65020; D65020.
DR RefSeq; NP_416948.4; NC_000913.3.
DR RefSeq; WP_001326575.1; NZ_LN832404.1.
DR AlphaFoldDB; P76553; -.
DR SMR; P76553; -.
DR BioGRID; 4262025; 9.
DR IntAct; P76553; 1.
DR STRING; 511145.b2453; -.
DR PaxDb; P76553; -.
DR PRIDE; P76553; -.
DR EnsemblBacteria; AAC75506; AAC75506; b2453.
DR EnsemblBacteria; BAA16331; BAA16331; BAA16331.
DR GeneID; 946233; -.
DR KEGG; ecj:JW2437; -.
DR KEGG; eco:b2453; -.
DR PATRIC; fig|1411691.4.peg.4287; -.
DR EchoBASE; EB3935; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_6; -.
DR InParanoid; P76553; -.
DR OMA; AKAMWIK; -.
DR PhylomeDB; P76553; -.
DR BioCyc; EcoCyc:G7283-MON; -.
DR UniPathway; UPA00560; -.
DR PRO; PR:P76553; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IMP:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Bacterial microcompartment; Iron; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..395
FT /note="Probable alcohol dehydrogenase EutG"
FT /id="PRO_0000087843"
FT BINDING 57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 116..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 156..160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 197..201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 281
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 295
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 295
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
FT BINDING 354
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0A9S1"
SQ SEQUENCE 395 AA; 41031 MW; 13875E8CDA5B5424 CRC64;
MQNELQTALF QAFDTLNLQR VKTFSVPPVT LCGPGSVSSC GQQAQTRGLK HLFVMADSFL
HQAGMTAGLT RSLTVKGIAM TLWPCPVGEP CITDVCAAVA QLRESGCDGV IAFGGGSVLD
AAKAVTLLVT NPDSTLAEMS ETSVLQPRLP LIAIPTTAGT GSETTNVTVI IDAVSGRKQV
LAHASLMPDV AILDAALTEG VPSHVTAMTG IDALTHAIEA YSALNATPFT DSLAIGAIAM
IGKSLPKAVG YGHDLAARES MLLASCMAGM AFSSAGLGLC HAMAHQPGAA LHIPHGLANA
MLLPTVMEFN RMVCRERFSQ IGRALRTKKS DDRDAINAVS ELIAEVGIGK RLGDVGATSA
HYGAWAQAAL EDICLRSNPR TASLEQIVGL YAAAQ
