ID   PCAF_PSEKB              Reviewed;         401 AA.
AC   Q8VPF1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Beta-ketoadipyl-CoA thiolase;
DE            EC=2.3.1.174;
DE   AltName: Full=3-oxoadipyl-CoA thiolase;
GN   Name=pcaF; Synonyms=catF;
OS   Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1301098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11741863; DOI=10.1128/jb.184.1.216-223.2002;
RA   Goebel M., Kassel-Cati K., Schmidt E., Reineke W.;
RT   "Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain
RT   B13: cloning, characterization, and analysis of sequences encoding 3-
RT   oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA
RT   thiolase.";
RL   J. Bacteriol. 184:216-223(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-19, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=11741862; DOI=10.1128/jb.184.1.207-215.2002;
RA   Kaschabek S.R., Kuhn B., Mueller D., Schmidt E., Reineke W.;
RT   "Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain
RT   B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A
RT   (CoA) transferase and 3-oxoadipyl-CoA thiolase.";
RL   J. Bacteriol. 184:207-215(2002).
CC   -!- FUNCTION: Catalyzes thiolytic cleavage of beta-ketoadipyl-CoA to
CC       succinyl-CoA and acetyl-CoA.
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         Evidence={ECO:0000269|PubMed:11741862};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.15 mM for 3-oxoadipyl-CoA {ECO:0000269|PubMed:11741862};
CC         KM=0.01 mM for CoA {ECO:0000269|PubMed:11741862};
CC       pH dependence:
CC         Optimum pH is 7.8. {ECO:0000269|PubMed:11741862};
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       acetyl-CoA and succinyl-CoA from 3-oxoadipate: step 2/2.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11741862}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; AY044272; AAL02407.1; -; Genomic_DNA.
DR   RefSeq; WP_043252818.1; NZ_HG322950.1.
DR   AlphaFoldDB; Q8VPF1; -.
DR   SMR; Q8VPF1; -.
DR   STRING; 1301098.PKB_2950; -.
DR   eggNOG; COG0183; Bacteria.
DR   OMA; QFLACNR; -.
DR   OrthoDB; 550338at2; -.
DR   SABIO-RK; Q8VPF1; -.
DR   UniPathway; UPA00157; UER00263.
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:0042952; P:beta-ketoadipate pathway; 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   1: Evidence at protein level;
KW   Acyltransferase; Aromatic hydrocarbons catabolism;
KW   Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11741862"
FT   CHAIN           2..401
FT                   /note="Beta-ketoadipyl-CoA thiolase"
FT                   /id="PRO_0000337672"
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;  41672 MW;  1A31D6FD41D25669 CRC64;
     MSREVYICDA VRTPIGRFGG SLAAVRADDL AAVPVKALVE RNPQVDWSQL DEVYLGCANQ
     AGEDNRNVAR MALLLAGLPD SVPGVTLNRL CASGMDAVGT AFRAIASGEA ELVIAGGVES
     MSRAPYVMGK ADSAFGRGQK IEDTTIGWRF INPLMKAQYG VDAMPETADN VADDYKVSRA
     DQDAFALRSQ QLAGRAQAAG YFAEEIVPVV IKGKKGETVV DADEHLRPDT TLEALAKLKP
     VNGPDKTVTA GNASGVNDGS VALILASAEA VKKHGLKARA KVLGMASAGV APRVMGIGPV
     PAVRKLLERL NLSVADFDVI ELNEAFAAQG LAVTRELGIA DDDARVNPNG GAIALGHPLG
     ASGARLVLTA VHQLEKSGGQ RGLCTMCVGV GQGVALAVER V