ID   PAAJ_ECOLX              Reviewed;         401 AA.
AC   P0C7L3; O53017; P77525;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Beta-ketoadipyl-CoA thiolase;
DE            EC=2.3.1.174;
DE   AltName: Full=3-oxoadipyl-CoA thiolase;
GN   Name=paaJ;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W / ATCC 11105 / DSM 1900 / 113-3;
RX   PubMed=9748275; DOI=10.1074/jbc.273.40.25974;
RA   Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M.,
RA   Garcia J.L., Diaz E.;
RT   "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a
RT   new aerobic hybrid pathway.";
RL   J. Biol. Chem. 273:25974-25986(1998).
CC   -!- FUNCTION: Catalyzes thiolytic cleavage of beta-ketoadipyl-CoA to
CC       succinyl-CoA and acetyl-CoA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA;
CC         Xref=Rhea:RHEA:19481, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57348; EC=2.3.1.174;
CC   -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; X97452; CAA66099.1; -; Genomic_DNA.
DR   RefSeq; WP_001206190.1; NZ_WVWF01000010.1.
DR   AlphaFoldDB; P0C7L3; -.
DR   SMR; P0C7L3; -.
DR   STRING; 585034.ECIAI1_1397; -.
DR   GeneID; 66674746; -.
DR   eggNOG; COG0183; Bacteria.
DR   OMA; MSRVPMW; -.
DR   UniPathway; UPA00930; -.
DR   GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR012793; PcaF.
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   TIGRFAMs; TIGR02430; pcaF; 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; Transferase.
FT   CHAIN           1..401
FT                   /note="Beta-ketoadipyl-CoA thiolase"
FT                   /id="PRO_0000337827"
FT   ACT_SITE        90
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        357
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        387
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   401 AA;  42277 MW;  0B62EBE2880FED14 CRC64;
     MREAFICDGI RTPIGRYGGA LSGVRADDLA AIPLRELLVR NPRLDAECID DVILGCANQA
     GEDNRNVARM ATLLAGLPQS VSGTTINRLC GSGLDALGFA ARAIKAGDGD LLIAGGVESM
     SRAPFVMGKA TSAFSRQAEM FDTTIGWRFV NPLMAQQFGT DSMPETAENV AELLKISRED
     QDSFALRSQQ RTAKAQSSGI LAEEIVPVVL KNKKGVVTEI QHDEHLRPET TLEQLRGLKA
     PFRANGVITA GNASGVNDGA AALIIASEQM AAAQGLTPRA RIVAMATAGV EPRLMGLGPV
     PATRRVLERA GLSIHDMDVI ELNEAFAAQA LGVLRELGLP DDAPHVNPNG GAIALGHPLG
     MSGARLALAA SHELHRRNGR YALCTMCIGV GQGIAMILER V