ID   CATF_ACIAD              Reviewed;         401 AA.
AC   Q43935;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Beta-ketoadipyl-CoA thiolase;
DE            EC=2.3.1.174;
DE   AltName: Full=3-oxoadipyl-CoA thiolase;
GN   Name=catF; OrderedLocusNames=ACIAD1450;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8125318; DOI=10.1016/0378-1119(94)90783-8;
RA   Shanley M.S., Harrison A., Parales R.E., Kowalchuk G., Mitchell D.J.,
RA   Ornston L.N.;
RT   "Unusual G + C content and codon usage in catIJF, a segment of the ben-cat
RT   supra-operonic cluster in the Acinetobacter calcoaceticus chromosome.";
RL   Gene 138:59-65(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; AF009224; AAC46434.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68313.1; -; Genomic_DNA.
DR   RefSeq; WP_004925437.1; NC_005966.1.
DR   AlphaFoldDB; Q43935; -.
DR   SMR; Q43935; -.
DR   STRING; 62977.ACIAD1450; -.
DR   EnsemblBacteria; CAG68313; CAG68313; ACIAD1450.
DR   GeneID; 45233862; -.
DR   KEGG; aci:ACIAD1450; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_2_2_6; -.
DR   OMA; QFLACNR; -.
DR   OrthoDB; 550338at2; -.
DR   BioCyc; ASP62977:ACIAD_RS06700-MON; -.
DR   UniPathway; UPA00157; UER00263.
DR   Proteomes; UP000000430; Chromosome.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..401
FT                   /note="Beta-ketoadipyl-CoA thiolase"
FT                   /id="PRO_0000206424"
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;  42051 MW;  132DF88770E786E0 CRC64;
     MKHAYIVDAI RTPFGRYAGG LAAVRADDLG AIPIAALIER NPSVNWAQVD DVIYGCANQA
     GEDNRNVGRM SALLAGLPVE VPATTVNRLC GSSLDAIAMA ARAIKAGEAH LIIAGGVESM
     SRAPYVMGKS EGAFGRTQKI EDTTMGWRFI NPKLKAMYGV DTMPQTAENV AEQFGIQRED
     QDQFAYTSQQ RTAAAQAKGY FAKEIVPVTI PQRKGEPVVI ATDEHPRAST TLEGLAKLKG
     VVKPEGSVTA GNASGINDGA AAVLIASDEA VAQYQLKARA KIIASTTVGI EPRIMGFAPA
     PAIKKLLKQA NLTLDQMDVI ELNEAFAAQA LACTRDLGLA DDDARVNPNG GAIALGHPLG
     ASGARLVTTA LNQLEQSGGK YALCSMCIGV GQGIALIIER V