EUTG_SALTY
ID EUTG_SALTY Reviewed; 395 AA.
AC P41795;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable alcohol dehydrogenase EutG {ECO:0000303|PubMed:7868611};
DE EC=1.1.1.1 {ECO:0000305|PubMed:7868611};
DE AltName: Full=Ethanolamine utilization protein EutG;
GN Name=eutG {ECO:0000303|PubMed:7868611}; OrderedLocusNames=STM2461;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=7868611; DOI=10.1128/jb.177.5.1357-1366.1995;
RA Stojiljkovic I., Baeumler A.J., Heffron F.;
RT "Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence,
RT protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG
RT eutH gene cluster.";
RL J. Bacteriol. 177:1357-1366(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=10464203; DOI=10.1128/jb.181.17.5317-5329.1999;
RA Kofoid E.C., Rappleye C.A., Stojiljkovic I., Roth J.R.;
RT "The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes
RT five homologues of carboxysome shell proteins.";
RL J. Bacteriol. 181:5317-5329(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION, PATHWAY, OPERON, AND INDUCTION BY ETHANOLAMINE AND COBALAMIN.
RC STRAIN=LT2;
RX PubMed=3045078; DOI=10.1128/jb.170.9.3855-3863.1988;
RA Roof D.M., Roth J.R.;
RT "Ethanolamine utilization in Salmonella typhimurium.";
RL J. Bacteriol. 170:3855-3863(1988).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA Penrod J.T., Roth J.R.;
RT "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT in Salmonella enterica.";
RL J. Bacteriol. 188:2865-2874(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=23585538; DOI=10.1128/jb.02179-12;
RA Huseby D.L., Roth J.R.;
RT "Evidence that a metabolic microcompartment contains and recycles private
RT cofactor pools.";
RL J. Bacteriol. 195:2864-2879(2013).
RN [7]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=29531136; DOI=10.1128/iai.00172-18;
RA Anderson C.J., Satkovich J., Koeseoglu V.K., Agaisse H., Kendall M.M.;
RT "The Ethanolamine Permease EutH Promotes Vacuole Adaptation of Salmonella
RT enterica and Listeria monocytogenes during Macrophage Infection.";
RL Infect. Immun. 86:0-0(2018).
CC -!- FUNCTION: Probably acts on the acetaldehyde produced by the degradation
CC of ethanolamine, producing ethanol. {ECO:0000305|PubMed:10464203,
CC ECO:0000305|PubMed:16585748, ECO:0000305|PubMed:7868611}.
CC -!- FUNCTION: Expression of the eut operon allows this bacteria to use
CC ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on
CC cobalamin (vitamin B12) both as a cofactor for the ethanolamine
CC ammonia-lyase (EAL) activity and to induce the operon (PubMed:3045078).
CC EA enhances bacterial survival in macrophages in a concentration-
CC dependent manner, suggesting it is an important nutrient during
CC infection (PubMed:29531136). {ECO:0000269|PubMed:29531136,
CC ECO:0000269|PubMed:3045078}.
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:10464203, ECO:0000305|PubMed:16585748,
CC ECO:0000305|PubMed:7868611};
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 {ECO:0000269|PubMed:3045078}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000305|PubMed:23585538}.
CC -!- INDUCTION: Part of the 17-gene eut operon transcribed from a single
CC promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl,
CC vitamin B12). {ECO:0000269|PubMed:3045078}.
CC -!- DISRUPTION PHENOTYPE: Unable to grow with ethanolamine (EA) as sole
CC carbon source. Slightly attenuated in a mouse model of infection
CC (PubMed:7868611). Not required for aerobic growth on EA supplemented
CC with cobalamin (vitamin B12). A double eutJ-eutG deletion is not
CC required for growth on EA supplemented with vitamin B12
CC (PubMed:10464203). A non-polar deletion mutant grows on EA at pH 5.5 to
CC pH 7.0 but not at pH 8.0 or pH 8.5, releases increased amounts of
CC acetaldehyde on EA plus vitamin B12. Preventing acetaldehyde vapor loss
CC allow growth up to pH 8.5 (PubMed:16585748).
CC {ECO:0000269|PubMed:10464203, ECO:0000269|PubMed:16585748,
CC ECO:0000269|PubMed:7868611}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U18560; AAA80211.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78120.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21355.1; -; Genomic_DNA.
DR RefSeq; NP_461396.1; NC_003197.2.
DR RefSeq; WP_001147500.1; NC_003197.2.
DR AlphaFoldDB; P41795; -.
DR SMR; P41795; -.
DR STRING; 99287.STM2461; -.
DR PaxDb; P41795; -.
DR EnsemblBacteria; AAL21355; AAL21355; STM2461.
DR GeneID; 1253983; -.
DR KEGG; stm:STM2461; -.
DR PATRIC; fig|99287.12.peg.2599; -.
DR HOGENOM; CLU_007207_0_0_6; -.
DR OMA; AKAMWIK; -.
DR PhylomeDB; P41795; -.
DR BioCyc; SENT99287:STM2461-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Bacterial microcompartment; Iron; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Virulence.
FT CHAIN 1..395
FT /note="Probable alcohol dehydrogenase EutG"
FT /id="PRO_0000087844"
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"
FT CONFLICT 199..200
FT /note="EG -> D (in Ref. 1; AAA80211 and 2; AAC78120)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..234
FT /note="NATPFTDSLA -> TPRRLPQPG (in Ref. 1; AAA80211 and 2;
FT AAC78120)"
FT /evidence="ECO:0000305"
FT CONFLICT 367..378
FT /note="QAALEDICLRSN -> RAGGYLSAQY (in Ref. 1; AAA80211 and
FT 2; AAC78120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 40903 MW; 200C136746F26CDE CRC64;
MQAELQTALF QAFDTLNLQR VKTFSVPPVT LCGLGALGAC GQEAQARGVS HLFVMVDSFL
HQAGMTAPLA RSLAMKGVAM TVWPCPPGEP CITDVCAAVA QLREAACDGV VAFGGGSVLD
AAKAVALLVT NPDQTLSAMT EHSTLRPRLP LIAVPTTAGT GSETTNVTVI IDAVSGRKQV
LAHASLMPDV AILDAAVTEG VPPNVTAMTG IDALTHAIEA YSALNATPFT DSLAIGAIAM
IGKSLPKAVG YGHDLAAREN MLLASCMAGM AFSSAGLGLC HAMAHQPGAA LHIPHGQANA
MLLPTVMGFN RMVCRERFSQ IGRALTNKKS DDRDAIAAVC ELIAEVGQSK RLADAGAKPE
HYSAWAQAAL EDICLRSNPR TATQAQIIDL YAAAG
