EUTE_SALTY
ID EUTE_SALTY Reviewed; 467 AA.
AC P41793;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Acetaldehyde dehydrogenase (acetylating) EutE {ECO:0000303|PubMed:21803884};
DE EC=1.2.1.10 {ECO:0000269|PubMed:21803884};
DE AltName: Full=Ethanolamine utilization protein EutE;
GN Name=eutE {ECO:0000303|PubMed:2656649}; OrderedLocusNames=STM2463;
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=2656649; DOI=10.1128/jb.171.6.3316-3323.1989;
RA Roof D.M., Roth J.R.;
RT "Functions required for vitamin B12-dependent ethanolamine utilization in
RT Salmonella typhimurium.";
RL J. Bacteriol. 171:3316-3323(1989).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=15466042; DOI=10.1128/jb.186.20.6885-6890.2004;
RA Penrod J.T., Mace C.C., Roth J.R.;
RT "A pH-sensitive function and phenotype: evidence that EutH facilitates
RT diffusion of uncharged ethanolamine in Salmonella enterica.";
RL J. Bacteriol. 186:6885-6890(2004).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16272400; DOI=10.1099/mic.0.28156-0;
RA Starai V.J., Garrity J., Escalante-Semerena J.C.;
RT "Acetate excretion during growth of Salmonella enterica on ethanolamine
RT requires phosphotransacetylase (EutD) activity, and acetate recapture
RT requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta)
RT activities.";
RL Microbiology 151:3793-3801(2005).
RN [8]
RP 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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RC STRAIN=LT2;
RX PubMed=21803884; DOI=10.1128/aem.05358-11;
RA Zhu H., Gonzalez R., Bobik T.A.;
RT "Coproduction of acetaldehyde and hydrogen during glucose fermentation by
RT Escherichia coli.";
RL Appl. Environ. Microbiol. 77:6441-6450(2011).
RN [10]
RP FUNCTION, AND 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 [11]
RP FUNCTION, INTERACTION WITH EUTS, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP BIOTECHNOLOGY.
RC STRAIN=LT2;
RX PubMed=27450681; DOI=10.1007/s00253-016-7737-8;
RA Quin M.B., Perdue S.A., Hsu S.Y., Schmidt-Dannert C.;
RT "Encapsulation of multiple cargo proteins within recombinant Eut
RT nanocompartments.";
RL Appl. Microbiol. Biotechnol. 100:9187-9200(2016).
RN [12]
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: Acts as the second step in ethanolamine degradation by
CC converting acetaldehyde into acetyl-CoA (Probable) (PubMed:21803884).
CC May play a role in bacterial microcompartment (BMC) assembly or
CC maintenance (Probable). Directly targeted to the BMC (PubMed:27450681).
CC {ECO:0000269|PubMed:21803884, ECO:0000269|PubMed:27450681,
CC ECO:0000305|PubMed:10464203, ECO:0000305|PubMed:23585538,
CC ECO:0000305|PubMed:2656649, ECO:0000305|PubMed:3045078}.
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=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.10;
CC Evidence={ECO:0000269|PubMed:21803884};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23289;
CC Evidence={ECO:0000269|PubMed:21803884};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23290;
CC Evidence={ECO:0000269|PubMed:21803884};
CC -!- COFACTOR:
CC Note=Has a very strong preference for NAD(+) over NADP(+) in both
CC catalytic directions. {ECO:0000269|PubMed:21803884};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.4 uM for acetyl-CoA {ECO:0000269|PubMed:21803884};
CC Vmax=69.91 umol/min/mg enzyme {ECO:0000269|PubMed:21803884};
CC pH dependence:
CC Optimum pH is 6.5 for acetyl-CoA reductase and 7.5 for acetaldehyde
CC dehydrogenase activities. {ECO:0000269|PubMed:21803884};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000269|PubMed:3045078}.
CC -!- SUBUNIT: Interacts with EutS, which targets it to the interior of the
CC BMC. {ECO:0000269|PubMed:27450681}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:27450681, ECO:0000305|PubMed:23585538}.
CC Note=Probably located inside the BMC. {ECO:0000305|PubMed:27450681}.
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 -!- DOMAIN: The first 21 residues target foreign proteins (tested with
CC eGFP) to the BMC in E.coli. The cargo is only detected by Western blot
CC in broken shells, strongly suggesting this protein is normally found
CC inside the BMC and not on its exterior. {ECO:0000269|PubMed:27450681}.
CC -!- DISRUPTION PHENOTYPE: Can use ethanolamine (EA) as a nitrogen source
CC but not as a carbon source. Slightly attenuated in a mouse model of
CC infection (PubMed:7868611, PubMed:2656649). No aerobic growth on EA
CC supplemented with cobalamin (vitamin B12) (PubMed:10464203,
CC PubMed:16272400). A non-polar deletion mutant does not grow on EA
CC between pH 5.5 and pH 8.5, releases increased amounts of acetaldehyde
CC on EA plus vitamin B12 (PubMed:16585748). A deletion allows growth on
CC acetate, suggesting BMC assembly or maintenance is impaired
CC (PubMed:23585538). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:16272400, ECO:0000269|PubMed:16585748,
CC ECO:0000269|PubMed:23585538, ECO:0000269|PubMed:2656649,
CC ECO:0000269|PubMed:7868611}.
CC -!- BIOTECHNOLOGY: Has been used to coproduce acetaldehyde and hydrogen in
CC E.coli. {ECO:0000269|PubMed:21803884}.
CC -!- BIOTECHNOLOGY: Artificial BMCs can be made in E.coli by expressing
CC eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins
CC can be targeted to them using the first 21 residues of this protein.
CC This can lead to the development of tailored BMCs for specific
CC metabolic reactions. {ECO:0000269|PubMed:27450681}.
CC -!- SIMILARITY: Belongs to the EutE/PduP family. {ECO:0000305}.
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DR EMBL; U18560; AAA80209.1; -; Genomic_DNA.
DR EMBL; AF093749; AAC78118.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21357.1; -; Genomic_DNA.
DR RefSeq; NP_461398.1; NC_003197.2.
DR RefSeq; WP_001075640.1; NC_003197.2.
DR AlphaFoldDB; P41793; -.
DR SMR; P41793; -.
DR STRING; 99287.STM2463; -.
DR PaxDb; P41793; -.
DR EnsemblBacteria; AAL21357; AAL21357; STM2463.
DR GeneID; 1253985; -.
DR KEGG; stm:STM2463; -.
DR PATRIC; fig|99287.12.peg.2601; -.
DR HOGENOM; CLU_028794_1_0_6; -.
DR OMA; IAIKSRN; -.
DR PhylomeDB; P41793; -.
DR BioCyc; MetaCyc:STM2463-MON; -.
DR BioCyc; SENT99287:STM2463-MON; -.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07121; ALDH_EutE; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR012408; Acetald_propionald_DH-rel.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036410; EutE_PduP; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; NAD; Oxidoreductase; Reference proteome;
KW Virulence.
FT CHAIN 1..467
FT /note="Acetaldehyde dehydrogenase (acetylating) EutE"
FT /id="PRO_0000087085"
FT REGION 1..19
FT /note="Targets protein to the BMC"
FT /evidence="ECO:0000269|PubMed:27450681"
FT CONFLICT 219
FT /note="A -> R (in Ref. 1; AAA80209 and 2; AAC78118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 49174 MW; 17ED20C841E1C336 CRC64;
MNQQDIEQVV KAVLLKMKDS SQPASTVHEM GVFASLDDAV AAAKRAQQGL KSVAMRQLAI
HAIREAGEKH ARELAELAVS ETGMGRVDDK FAKNVAQARG TPGVECLSPQ VLTGDNGLTL
IENAPWGVVA SVTPSTNPAA TVINNAISLI AAGNSVVFAP HPAAKKVSQR AITLLNQAVV
AAGGPENLLV TVANPDIETA QRLFKYPGIG LLVVTGGEAV VDAARKHTNK RLIAAGAGNP
PVVVDETADL PRAAQSIVKG ASFDNNIICA DEKVLIVVDS VADELMRLME GQHAVKLTAA
QAEQLQPVLL KNIDERGKGT VSRDWVGRDA GKIAAAIGLN VPDQTRLLFV ETPANHPFAV
TEMMMPVLPV VRVANVEEAI ALAVQLEGGC HHTAAMHSRN IDNMNQMANA IDTSIFVKNG
PCIAGLGLGG EGWTTMTITT PTGEGVTSAR TFVRLRRCVL VDAFRIV
