AC MF_01618; DC Protein; auto TR HAMAP; MF_01618; -; 1; level=0 XX Names: FadI XX ID FADI DE RecName: Full=3-ketoacyl-CoA thiolase; DE EC=2.3.1.16; DE AltName: Full=ACSs; DE AltName: Full=Acetyl-CoA acyltransferase; DE AltName: Full=Acyl-CoA ligase; DE AltName: Full=Beta-ketothiolase; DE AltName: Full=Fatty acid oxidation complex subunit beta; GN Name=fadI; XX 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. 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 -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains CC (FadI). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. XX DR PROSITE; PS00098; THIOLASE_1; 1; trigger=no DR PROSITE; PS00737; THIOLASE_2; 1; trigger=no DR PROSITE; PS00099; THIOLASE_3; 1; trigger=no DR Pfam; PF02803; Thiolase_C; 1; trigger=no DR Pfam; PF00108; Thiolase_N; 1; trigger=no DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1; trigger=no DR NCBIfam; TIGR02446; FadI; 1; trigger=no XX KW Cytoplasm KW Acyltransferase KW Fatty acid metabolism KW Lipid degradation KW Lipid metabolism KW Transferase XX GO GO:0003988; F:acetyl-CoA C-acyltransferase activity GO GO:0006631; P:fatty acid metabolic process GO GO:0016042; P:lipid catabolic process GO GO:0005737; C:cytoplasm XX FT From: FADI_ECOLI (P76503) FT ACT_SITE 99 FT /note="Acyl-thioester intermediate" FT Condition: C FT ACT_SITE 392 FT /note="Proton acceptor" FT Condition: H FT ACT_SITE 422 FT /note="Proton acceptor" FT Condition: C XX Size: 435-442; Related: None; Template: P76503; Scope: Bacteria; Gammaproteobacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.20 2023/06/01 //