ID   PCAF_PSEAE              Reviewed;         401 AA.
AC   Q9I6R0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Beta-ketoadipyl-CoA thiolase;
DE            EC=2.3.1.174;
DE   AltName: Full=3-oxoadipyl-CoA thiolase;
GN   Name=pcaF; OrderedLocusNames=PA0228;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; beta-ketoadipate pathway;
CC       acetyl-CoA and succinyl-CoA from 3-oxoadipate: step 2/2.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG03617.1; -; Genomic_DNA.
DR   PIR; D83618; D83618.
DR   RefSeq; NP_248919.1; NC_002516.2.
DR   RefSeq; WP_003101891.1; NZ_QZGE01000024.1.
DR   AlphaFoldDB; Q9I6R0; -.
DR   SMR; Q9I6R0; -.
DR   STRING; 287.DR97_3185; -.
DR   PaxDb; Q9I6R0; -.
DR   EnsemblBacteria; AAG03617; AAG03617; PA0228.
DR   GeneID; 877715; -.
DR   KEGG; pae:PA0228; -.
DR   PATRIC; fig|208964.12.peg.238; -.
DR   PseudoCAP; PA0228; -.
DR   HOGENOM; CLU_031026_2_2_6; -.
DR   InParanoid; Q9I6R0; -.
DR   OMA; NASPMND; -.
DR   PhylomeDB; Q9I6R0; -.
DR   BioCyc; PAER208964:G1FZ6-230-MON; -.
DR   UniPathway; UPA00157; UER00263.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
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; Aromatic hydrocarbons catabolism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..401
FT                   /note="Beta-ketoadipyl-CoA thiolase"
FT                   /id="PRO_0000287819"
FT   ACT_SITE        91
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;  42106 MW;  BF8DF2798448D4DC CRC64;
     MSREVFICDA VRTPIGRFGG SLSAVRADDL AAVPLKALVE RNPGVDWSAL DEVFLGCANQ
     AGEDNRNVAR MALLLAGLPE SVPGVTLNRL CASGMDAIGT AFRAIACGEM ELAIAGGVES
     MSRAPYVMGK ADSAFGRGQK IEDTTIGWRF VNPLMKEQYG IDPMPQTADN VADDYRVSRA
     DQDAFALRSQ QRAGRAQEAG FFAEEIVPVT IRGRKGDTLV EHDEHPRPDT TLEALARLKP
     VNGPEKTVTA GNASGVNDGA AALVLASAEA VEKHGLTPRA RVLGMASAGV APRIMGIGPV
     PAVRKLLRRL DLAIDAFDVI ELNEAFASQG LACLRELGVA DDSEKVNPNG GAIALGHPLG
     MSGARLVLTA LHQLEKSGGR RGLATMCVGV GQGLALAIER V