ID   FADA_PSEOL              Reviewed;         391 AA.
AC   Q93Q11;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE            EC=2.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01620};
DE   AltName: Full=Acetyl-CoA acyltransferase {ECO:0000255|HAMAP-Rule:MF_01620};
DE   AltName: Full=Beta-ketothiolase {ECO:0000255|HAMAP-Rule:MF_01620};
DE   AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01620};
GN   Name=fadA {ECO:0000255|HAMAP-Rule:MF_01620};
OS   Pseudomonas oleovorans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=301;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29347 / CIP 105816 / NRRL B-14683 / TF4-1L;
RX   PubMed=12115060; DOI=10.1007/s00203-002-0444-0;
RA   Fiedler S., Steinbuchel A., Rehm B.H.;
RT   "The role of the fatty acid beta-oxidation multienzyme complex from
RT   Pseudomonas oleovorans in polyhydroxyalkanoate biosynthesis: molecular
RT   characterization of the fadBA operon from P. oleovorans and of the enoyl-
RT   CoA hydratase genes phaJ from P. oleovorans and Pseudomonas putida.";
RL   Arch. Microbiol. 178:149-160(2002).
CC   -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in which
CC       acetyl-CoA is released and the CoA ester of a fatty acid two carbons
CC       shorter is formed. {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01620};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC       (FadA). {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01620}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01620}.
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DR   EMBL; AF288535; AAK83059.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93Q11; -.
DR   SMR; Q93Q11; -.
DR   STRING; 301.JNHE01000003_gene1892; -.
DR   PRIDE; Q93Q11; -.
DR   eggNOG; COG0183; Bacteria.
DR   UniPathway; UPA00659; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   HAMAP; MF_01620; FadA; 1.
DR   InterPro; IPR012805; FadA.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_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; TIGR02445; fadA; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Fatty acid metabolism; Lipid degradation;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..391
FT                   /note="3-ketoacyl-CoA thiolase"
FT                   /id="PRO_0000206381"
FT   ACT_SITE        95
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ   SEQUENCE   391 AA;  41645 MW;  D7CAE2F37ED170A1 CRC64;
     MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNDKVD PKEVEDVIWG
     CVNQTLEQGW NIARMASLMT QIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TGNGDVFVVG
     GVEHMGHVSM MHGVDPNPHL SLHAAKASGM MGLTAEMLGK MHGITREQQD LFGLRSHQLA
     HKATVEGKFK DEIIPMQGYD ENGFLKVFDF DETIRPETTL EGLASLKPAF NPKGGTVTAG
     TSSQITDGAS CMVVMSGQRA MDLGIQPLAV IRSMAVAGVD PAIMGYGPVP STQKALKRAG
     LTMADIDFIE LNEAFAAQAL PVLKDLKVLD KMDEKVNLHG GAIALGHPFG CSGARISGTL
     LNVMKQNGGT LGVATMCVGL GQGITTVFER I