ID   FADA_SHEB8              Reviewed;         387 AA.
AC   A6WH99;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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};
GN   OrderedLocusNames=Shew185_0015;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000753; ABS06188.1; -; Genomic_DNA.
DR   RefSeq; WP_006083808.1; NC_009665.1.
DR   AlphaFoldDB; A6WH99; -.
DR   SMR; A6WH99; -.
DR   GeneID; 45040449; -.
DR   KEGG; sbm:Shew185_0015; -.
DR   HOGENOM; CLU_031026_2_3_6; -.
DR   OMA; YAYESHQ; -.
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; 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; TIGR02445; fadA; 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; Cytoplasm; Fatty acid metabolism; Lipid degradation;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..387
FT                   /note="3-ketoacyl-CoA thiolase"
FT                   /id="PRO_0000323554"
FT   ACT_SITE        91
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        343
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
FT   ACT_SITE        373
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01620"
SQ   SEQUENCE   387 AA;  40576 MW;  D8BE5A3984D9C175 CRC64;
     MKQAVIVDCI RTPMGRSKAG VFRNVRAETL SAELMKGLLL RNPQLDPNLI EDVIWGCVQQ
     TLEQGFNIAR NASLLAGIPK TAGAVTVNRL CGSSMDAIHQ AARAIMTGMG DTFIIGGVEH
     MGHVPMSHGV DFHPGLANNV AKASGMMGLT AEMLGKLHGI TREQQDAFAV RSHQRAYAAT
     VEGRFAKEIY GIEGHDANGA LIKVLQDEVI RPETTMESLA ALRPVFDPVN GTVTAGTSSA
     LSDGASAMLI MEESKARALG LPIRARIRSM AVAGCDAAIM GYGPVPATQK ALARAGITVA
     DLDVIELNEA FAAQSLPCVK DLGLADVVDD KINLNGGAIA LGHPLGCSGA RISTTLINLM
     EDKDATLGLA TMCIGLGQGI ATVFERV