EUTD_SALTY
ID EUTD_SALTY Reviewed; 338 AA.
AC P41790;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Phosphate acetyltransferase EutD;
DE EC=2.3.1.8 {ECO:0000269|PubMed:14996820};
DE AltName: Full=Ethanolamine utilization protein EutD;
DE AltName: Full=Phosphotransacetylase EutD {ECO:0000303|PubMed:16272400};
DE Short=PATC EutD;
GN Name=eutD {ECO:0000303|PubMed:2656649};
GN Synonyms=eutI {ECO:0000303|PubMed:7868611}; OrderedLocusNames=STM2466;
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], 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 96-338.
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 [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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=LT2;
RX PubMed=14996820; DOI=10.1128/jb.186.6.1890-1892.2004;
RA Brinsmade S.R., Escalante-Semerena J.C.;
RT "The eutD gene of Salmonella enterica encodes a protein with
RT phosphotransacetylase enzyme activity.";
RL J. Bacteriol. 186:1890-1892(2004).
RN [7]
RP FUNCTION, AND 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 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 [9]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [10]
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: Required for the use of ethanolamide (EA) as carbon, but not
CC nitrogen, source (Probable). Involved in acetate metabolism during
CC growth on EA, when expressed independently of the eut operon it can
CC restore growth to a double pta-acs deletion mutant (PubMed:14996820).
CC Required for acetate excretion during growth on EA (PubMed:16272400).
CC {ECO:0000269|PubMed:14996820, ECO:0000269|PubMed:16272400,
CC ECO:0000305|PubMed:2656649}.
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=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC Evidence={ECO:0000269|PubMed:14996820};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=46 uM for CoA {ECO:0000269|PubMed:14996820};
CC KM=129 uM for acetyl phosphate {ECO:0000269|PubMed:14996820};
CC Note=kcat is 1927 sec(-1). {ECO:0000269|PubMed:14996820};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:14996820};
CC -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC {ECO:0000269|PubMed:3045078}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P77218}.
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: Can use ethanolamine (EA) as a nitrogen source
CC but not as a carbon source (PubMed:2656649, PubMed:23585538). Not
CC required for aerobic growth on EA supplemented with cobalamin (vitamin
CC B12); deletions and mutations in this gene probably have polar effects
CC on downstream gene expression. A double eutD-eutM and a quadruple eutP-
CC eutQ-eutT-eutD deletion are not required for growth in the above
CC conditions (PubMed:10464203). Somewhat reduced growth on EA, no
CC excretion of acetate from cells. Reduced growth is due to residual
CC nutrients from rich medium (PubMed:16272400, PubMed:23585538). A non-
CC polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5,
CC releases slightly increased amounts of acetaldehyde on EA plus vitamin
CC B12 (PubMed:16585748). {ECO:0000269|PubMed:10464203,
CC ECO:0000269|PubMed:16272400, ECO:0000269|PubMed:16585748,
CC ECO:0000269|PubMed:23585538, ECO:0000269|PubMed:2656649}.
CC -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC butyryltransferase family. {ECO:0000305}.
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DR EMBL; AF093749; AAC78115.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21360.1; -; Genomic_DNA.
DR EMBL; U18560; AAA80206.1; -; Genomic_DNA.
DR RefSeq; NP_461401.1; NC_003197.2.
DR RefSeq; WP_000582931.1; NC_003197.2.
DR AlphaFoldDB; P41790; -.
DR SMR; P41790; -.
DR STRING; 99287.STM2466; -.
DR PaxDb; P41790; -.
DR EnsemblBacteria; AAL21360; AAL21360; STM2466.
DR GeneID; 1253988; -.
DR KEGG; stm:STM2466; -.
DR PATRIC; fig|99287.12.peg.2604; -.
DR HOGENOM; CLU_019723_0_1_6; -.
DR OMA; TMLVKMG; -.
DR PhylomeDB; P41790; -.
DR BioCyc; SENT99287:STM2466-MON; -.
DR BRENDA; 2.3.1.8; 2169.
DR UniPathway; UPA00560; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR InterPro; IPR012147; P_Ac_Bu_trans.
DR InterPro; IPR004614; P_AcTrfase.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF000428; P_Ac_trans; 1.
DR TIGRFAMs; TIGR00651; pta; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Bacterial microcompartment; Reference proteome;
KW Transferase; Virulence.
FT CHAIN 1..338
FT /note="Phosphate acetyltransferase EutD"
FT /id="PRO_0000179156"
FT CONFLICT 96..98
FT /note="AVE -> GID (in Ref. 3; AAA80206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36266 MW; B83D0D09E01EAE4C CRC64;
MIIERARELA VRAPARVVFP DALDERVLKA AHYLQQYGLA RPVLVASPFA LRQFALSHRM
AMDGIQVIDP HSNLSMRQRF AQRWLARAGE KTPPDAVEKL SDPLMFAAAM VSAGEADVCI
AGNLSSTANV LRAGLRVIGL QPGCKTLSSI FLMLPQYAGP ALGFADCSVV PQPTAAQLAD
IALASADTWR AITGEEPRVA MLSFSSNGSA RHPNVANVQQ ATELVRERAP QLLVDGELQF
DAAFVPEVAA QKAPDSPLQG RANVMIFPSL EAGNIGYKIT QRLGGYRAVG PLIQGLAAPL
HDLSRGCSVQ EIIELALVAA VPRQADVSRE RSLHTLVE
