EUTD_ECOLI
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 03-AUG-2022, entry version 136.
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; 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, 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_LN832404.1.
DR PDB; 1VMI; X-ray; 2.32 A; A=2-338.
DR PDBsum; 1VMI; -.
DR AlphaFoldDB; P77218; -.
DR SMR; P77218; -.
DR BioGRID; 4260920; 9.
DR BioGRID; 851279; 2.
DR IntAct; P77218; 7.
DR STRING; 511145.b2458; -.
DR PaxDb; P77218; -.
DR PRIDE; P77218; -.
DR EnsemblBacteria; AAC75511; AAC75511; b2458.
DR EnsemblBacteria; BAA16336; BAA16336; BAA16336.
DR GeneID; 946940; -.
DR KEGG; ecj:JW2442; -.
DR KEGG; eco:b2458; -.
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; TMLVKMG; -.
DR PhylomeDB; P77218; -.
DR BioCyc; EcoCyc:G7288-MON; -.
DR BioCyc; MetaCyc:G7288-MON; -.
DR UniPathway; UPA00560; -.
DR EvolutionaryTrace; P77218; -.
DR PRO; PR:P77218; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008959; F:phosphate acetyltransferase 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 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 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 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..137
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
