ID   YQEF_ECOLI              Reviewed;         393 AA.
AC   Q46939; Q2M9Z3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   Name=yqeF; OrderedLocusNames=b2844, JW5453;
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 / 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   [2]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40491.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U29581; AAB40491.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75883.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76913.1; -; Genomic_DNA.
DR   PIR; E65067; E65067.
DR   RefSeq; NP_417321.2; NC_000913.3.
DR   RefSeq; WP_000656030.1; NZ_LN832404.1.
DR   AlphaFoldDB; Q46939; -.
DR   SMR; Q46939; -.
DR   BioGRID; 4263512; 12.
DR   BioGRID; 851651; 1.
DR   DIP; DIP-12853N; -.
DR   STRING; 511145.b2844; -.
DR   jPOST; Q46939; -.
DR   PaxDb; Q46939; -.
DR   PRIDE; Q46939; -.
DR   EnsemblBacteria; AAC75883; AAC75883; b2844.
DR   EnsemblBacteria; BAE76913; BAE76913; BAE76913.
DR   GeneID; 947324; -.
DR   KEGG; ecj:JW5453; -.
DR   KEGG; eco:b2844; -.
DR   PATRIC; fig|1411691.4.peg.3890; -.
DR   EchoBASE; EB2900; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_0_0_6; -.
DR   InParanoid; Q46939; -.
DR   OMA; ICPSIAI; -.
DR   PhylomeDB; Q46939; -.
DR   BioCyc; EcoCyc:G7464-MON; -.
DR   PRO; PR:Q46939; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IMP:EcoCyc.
DR   GO; GO:0071271; P:1-butanol biosynthetic process; IMP:CACAO.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..393
FT                   /note="Probable acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000206456"
FT   ACT_SITE        88
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   393 AA;  41019 MW;  FF21A11064A9B88B CRC64;
     MKDVVIVGAL RTPIGCFRGA LAGHSAVELG SLVVKALIER TGVPAYAVDE VILGQVLTAG
     AGQNPARQSA IKGGLPNSVS AITINDVCGS GLKALHLATQ AIQCGEADIV IAGGQENMSR
     APHVLTDSRT GAQLGNSQLV DSLVHDGLWD AFNDYHIGVT AENLAREYGI SRQLQDAYAL
     SSQQKARAAI DAGRFKDEIV PVMTQSNGQT LVVDTDEQPR TDASAEGLAR LNPSFDSLGS
     VTAGNASSIN DGAAAVMMMS EAKARALNLP VLARIRAFAS VGVDPALMGI APVYATRRCL
     ERVGWQLAEV DLIEANEAFA AQALSVGKML EWDERRVNVN GGAIALGHPI GASGCRILVS
     LVHEMVKRNA RKGLATLCIG GGQGVALTIE RDE