ID   PCAF_PSEPU              Reviewed;         400 AA.
AC   Q51956;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Beta-ketoadipyl-CoA thiolase;
DE            EC=2.3.1.174;
DE   AltName: Full=3-oxoadipyl-CoA thiolase;
GN   Name=pcaF;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PRS2000;
RX   PubMed=7961399; DOI=10.1128/jb.176.21.6479-6488.1994;
RA   Harwood C.S., Nichols N.N., Kim M.-K., Ditty J.L., Parales R.E.;
RT   "Identification of the pcaRKF gene cluster from Pseudomonas putida:
RT   involvement in chemotaxis, biodegradation, and transport of 4-
RT   hydroxybenzoate.";
RL   J. Bacteriol. 176:6479-6488(1994).
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   -!- 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; U10895; AAA85138.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q51956; -.
DR   SMR; Q51956; -.
DR   STRING; 1240350.AMZE01000001_gene2841; -.
DR   eggNOG; COG0183; Bacteria.
DR   BioCyc; MetaCyc:MON-3207; -.
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   3: Inferred from homology;
KW   Acyltransferase; Aromatic hydrocarbons catabolism; Transferase.
FT   CHAIN           1..400
FT                   /note="Beta-ketoadipyl-CoA thiolase"
FT                   /id="PRO_0000206422"
FT   ACT_SITE        90
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   400 AA;  41781 MW;  856336E2E48152B2 CRC64;
     MRDVFICDAI RTPIGRFGGA LAGVRADDLA AVPLKALIEP NPAVQWDQVD EVFFGCANQA
     GEDNRNVARM ALLLAGLPES IPGVTLNRLC ASGMDAIGTA FRAIASGEME LAIAGGVESM
     SRAPFVMGKA ESGYSRNMKL EDTTIGWRFI NPLMKSQYGV DSMPETADNV ADDYQVSRAD
     QDAFALRSQQ KAAAAQAAGF FAEEIVPVRI AHKKGETIVE RDEHLRPETT LEALTKLKPV
     NGPDKTVTAG NASGVNDGAA ALILASAEAV KKHGLTPRAR VLGMASGGVA PRVMGIGPVP
     AVRKLTERLG VAVSDFDVIE LNEAFASQGL AVLRELGVAD DAPQVNPNGG AIALGHPLGM
     SGARLVLTAL HQLEKSGGRK GLATMCVGVG QGLALAIERV