ID   FADA_PSEPU              Reviewed;         391 AA.
AC   Q9R9W0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 90.
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 putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=U;
RX   PubMed=10506180; DOI=10.1074/jbc.274.41.29228;
RA   Garcia B., Olivera E.R., Minambres B., Fernandez-Valverde M., Canedo L.M.,
RA   Prieto M.A., Garcia J.L., Martinez M., Luengo J.M.;
RT   "Novel biodegradable aromatic plastics from a bacterial source. Genetic and
RT   biochemical studies on a route of the phenylacetyl-CoA catabolon.";
RL   J. Biol. Chem. 274:29228-29241(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=U;
RX   PubMed=11251808; DOI=10.1046/j.1365-2958.2001.02296.x;
RA   Olivera E.R., Carnicero D., Garcia B., Minambres B., Moreno M.A.,
RA   Canedo L., Dirusso C.C., Naharro G., Luengo J.M.;
RT   "Two different pathways are involved in the beta-oxidation of n-alkanoic
RT   and n-phenylalkanoic acids in Pseudomonas putida U: genetic studies and
RT   biotechnological applications.";
RL   Mol. Microbiol. 39:863-874(2001).
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; AF150672; AAF02534.1; -; Genomic_DNA.
DR   EMBL; AF290949; AAK18168.1; -; Genomic_DNA.
DR   RefSeq; WP_016500745.1; NZ_WOWR01000052.1.
DR   AlphaFoldDB; Q9R9W0; -.
DR   SMR; Q9R9W0; -.
DR   STRING; 1240350.AMZE01000003_gene3076; -.
DR   GeneID; 45525197; -.
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_0000206382"
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;  41614 MW;  EEB2DCE65EAE51D6 CRC64;
     MSLNPRDVVI VDFGRTPMGR SKGGMHRNTR AEDMSAHLIS KLLERNDKVD PKEVEDVIWG
     CVNQTLEQGW NIARMASLMT PIPHTSAAQT VSRLCGSSMS ALHTAAQAIM TGNGDVFVIG
     GVEHMGHVSM MHGVDPNPHL SLHAAKASGM MGLTAEMLGK MHGITREQQD LFGVRSHQLA
     HKATVEGKFK DEIIPMQGYD ENGFLKVFDF DETIRPETTL EGLASLKPAF NPKGGTVTAG
     TSSQITDGAS CMIVMSGQRA MDLGIQPLAV IRSMAVAGVD PAIMGYGPVP STQKALKRAG
     LTMADIDFIE LNEAFAAQAL PVLKDLKVLD KMDEKVNLHG GAIALGHPFG CSGARISGTL
     LNVMKQNGGT LGVATMCVGL GQGITTVFER V