ID   EUTD_ECOLI              Reviewed;         338 AA.
AC   P77218;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   10-JUN-2026, entry version 150.
DE   RecName: Full=Phosphate acetyltransferase EutD;
DE            EC=2.3.1.8 {ECO:0000269|PubMed:21046341};
DE   AltName: Full=Ethanolamine utilization protein EutD;
GN   Name=eutD; Synonyms=eutI, ypfA; OrderedLocusNames=b2458, JW2442;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND POSSIBLE SUBCELLULAR LOCATION.
RC   STRAIN=K12 / AG1;
RX   PubMed=21046341; DOI=10.1007/s12275-010-0091-0;
RA   Bologna F.P., Campos-Bermudez V.A., Saavedra D.D., Andreo C.S.,
RA   Drincovich M.F.;
RT   "Characterization of Escherichia coli EutD: a phosphotransacetylase of the
RT   ethanolamine operon.";
RL   J. Microbiol. 48:629-636(2010).
RN   [5] {ECO:0007744|PDB:1VMI}
RP   X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 2-338.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RG   Joint center for structural genomics (JCSG);
RT   "Crystal structure of Putative phosphate acetyltransferase (np_416953.1)
RT   from Escherichia coli k12 at 2.32 A resolution.";
RL   Submitted (SEP-2004) to the PDB data bank.
CC   -!- FUNCTION: When expressed independently of the eut operon it can restore
CC       growth to a double pta-acs deletion mutant.
CC       {ECO:0000269|PubMed:21046341}.
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:21046341};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19522;
CC         Evidence={ECO:0000269|PubMed:21046341};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19523;
CC         Evidence={ECO:0000269|PubMed:21046341};
CC   -!- ACTIVITY REGULATION: Activated by pyruvate, unaffected by NADH, ATP and
CC       PEP, unlike Pta. {ECO:0000269|PubMed:21046341}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=311.7 uM for acetyl phosphate {ECO:0000269|PubMed:21046341};
CC         KM=32.7 uM for CoA {ECO:0000269|PubMed:21046341};
CC         KM=9.5 uM for acetyl-CoA {ECO:0000269|PubMed:21046341};
CC         Note=kcat is 415.5 sec(-1) for acetyl-CoA formation, kcat is 119.8
CC         sec(-1) for acetyl phosphate formation.
CC         {ECO:0000269|PubMed:21046341};
CC       pH dependence:
CC         Optimum pH is 7.8. {ECO:0000269|PubMed:21046341};
CC   -!- PATHWAY: Amine and polyamine degradation; ethanolamine degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21046341}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21046341}. Note=It
CC       is not clear if this enzyme is found in the cytoplasm or the bacterial
CC       microcompartment. {ECO:0000305|PubMed:21046341}.
CC   -!- SIMILARITY: Belongs to the phosphate acetyltransferase and
CC       butyryltransferase 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; AAC75511.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16336.1; -; Genomic_DNA.
DR   PIR; A65021; A65021.
DR   RefSeq; NP_416953.1; NC_000913.3.
DR   RefSeq; WP_000582977.1; NZ_CP009789.1.
DR   PDB; 1VMI; X-ray; 2.32 A; A=2-338.
DR   AlphaFoldDB; P77218; -.
DR   SMR; P77218; -.
DR   BioGRID; 4260920; 14.
DR   BioGRID; 851279; 2.
DR   FunCoup; P77218; 349.
DR   IntAct; P77218; 7.
DR   STRING; 511145.b2458; -.
DR   PaxDb; 511145-b2458; -.
DR   EnsemblBacteria; AAC75511; AAC75511; b2458.
DR   GeneID; 75172563; -.
DR   GeneID; 946940; -.
DR   KEGG; ecj:JW2442; -.
DR   KEGG; eco:b2458; -.
DR   KEGG; ecoc:C3026_13640; -.
DR   PATRIC; fig|1411691.4.peg.4282; -.
DR   EchoBASE; EB3940; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_019723_0_1_6; -.
DR   InParanoid; P77218; -.
DR   OMA; CEYGENG; -.
DR   OrthoDB; 9808984at2; -.
DR   PhylomeDB; P77218; -.
DR   BioCyc; EcoCyc:G7288-MONOMER; -.
DR   BioCyc; MetaCyc:G7288-MONOMER; -.
DR   UniPathway; UPA00560; -.
DR   EvolutionaryTrace; P77218; -.
DR   PRO; PR:P77218; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008959; F:phosphate acetyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0046336; P:ethanolamine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR   FunFam; 3.40.50.10750:FF:000001; Phosphate acetyltransferase; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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; IPR050500; Phos_Acetyltrans/Butyryltrans.
DR   InterPro; IPR002505; PTA_PTB.
DR   NCBIfam; NF007233; PRK09653.1; 1.
DR   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF1; PHOSPHATE ACETYLTRANSFERASE EUTD; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PDBsum; 1VMI; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..338
FT                   /note="Phosphate acetyltransferase EutD"
FT                   /id="PRO_0000179155"
FT   HELIX           2..7
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           8..11
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          16..20
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           25..36
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          41..46
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           48..58
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           74..88
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           96..99
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           103..112
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           127..133
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           134..138
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          148..158
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          162..169
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           175..193
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           213..228
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          232..238
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           240..244
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           246..252
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   TURN            257..260
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          263..266
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           270..284
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          286..298
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:1VMI"
FT   HELIX           309..320
FT                   /evidence="ECO:0007829|PDB:1VMI"
SQ   SEQUENCE   338 AA;  36067 MW;  781B1FCB1298AA83 CRC64;
     MIIERCRELA LRAPARVVFP DALDQRVLKA AQYLHQQGLA TPILVANPFE LRQFALSHGV
     AMDGLQVIDP HGNLAMREEF AHRWLARAGE KTPPDALEKL TDPLMFAAAM VSAGKADVCI
     AGNLSSTANV LRAGLRIIGL QPGCKTLSSI FLMLPQYSGP ALGFADCSVV PQPTAAQLAD
     IALASAETWR AITGEEPRVA MLSFSSNGSA RHPCVANVQQ ATEIVRERAP KLVVDGELQF
     DAAFVPEVAA QKAPASPLQG KANVMVFPSL EAGNIGYKIA QRLGGYRAVG PLIQGLAAPM
     HDLSRGCSVQ EIIELALVAA VPRQTEVNRE SSLQTLVE
//