ID A0AAP2G7M6_9GAMM Unreviewed; 387 AA. AC A0AAP2G7M6; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. DE RecName: Full=3-ketoacyl-CoA thiolase {ECO:0000256|HAMAP-Rule:MF_01620}; DE EC=2.3.1.16 {ECO:0000256|HAMAP-Rule:MF_01620}; DE AltName: Full=Acetyl-CoA acyltransferase {ECO:0000256|HAMAP-Rule:MF_01620}; DE AltName: Full=Beta-ketothiolase {ECO:0000256|HAMAP-Rule:MF_01620}; DE AltName: Full=Fatty acid oxidation complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01620}; GN Name=fadA {ECO:0000256|HAMAP-Rule:MF_01620, GN ECO:0000313|EMBL:MBT1486996.1}; GN ORFNames=IAF07_01015 {ECO:0000313|EMBL:MBT1486996.1}, JRZ91_01015 GN {ECO:0000313|EMBL:QVH72005.1}; OS Dickeya dianthicola. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Dickeya. OX NCBI_TaxID=204039 {ECO:0000313|EMBL:MBT1486996.1, ECO:0000313|Proteomes:UP000811537}; RN [1] {ECO:0000313|EMBL:MBT1486996.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=16LI01 {ECO:0000313|EMBL:QVH72005.1}, and DDI_59W RC {ECO:0000313|EMBL:MBT1486996.1}; RA Ge T.; RT "Pangenomic Analysis of Dickeya dianthicola Strains Reveals the Outbreak of RT Blackleg and Soft Rot of Potato in USA."; RL Submitted (MAY-2021) 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:0000256|HAMAP-Rule:MF_01620}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an acyl-CoA + acetyl-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:0000256|HAMAP-Rule:MF_01620}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000256|HAMAP-Rule:MF_01620}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains CC (FadA). {ECO:0000256|HAMAP-Rule:MF_01620}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01620}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|HAMAP-Rule:MF_01620, CC ECO:0000256|RuleBase:RU003557}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAHEPW010000002; MBT1486996.1; -; Genomic_DNA. DR EMBL; CP069603; QVH72005.1; -; Genomic_DNA. DR RefSeq; WP_024109303.1; NZ_WABK01000117.1. DR GeneID; 49320133; -. DR Proteomes; UP000676146; Chromosome. DR Proteomes; UP000811537; Unassembled WGS sequence. DR CDD; cd00751; thiolase; 1. DR FunFam; 3.40.47.10:FF:000010; Acetyl-CoA acetyltransferase (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; IPR050215; Thiolase-like_sf_Thiolase. 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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1. DR NCBIfam; TIGR02445; fadA; 1. DR PANTHER; PTHR43853:SF11; 3-KETOACYL-COA THIOLASE FADA; 1. DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. 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 {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_01620}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01620}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP- KW Rule:MF_01620}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP- KW Rule:MF_01620}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_01620}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01620}. FT DOMAIN 5..254 FT /note="Thiolase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 262..386 FT /note="Thiolase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02803" FT ACT_SITE 91 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620" FT ACT_SITE 343 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620" FT ACT_SITE 373 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01620" SQ SEQUENCE 387 AA; 40656 MW; 513EEEE882E2A713 CRC64; MENAVIVDAV RTPMGRSKGG AFRQVRAETL SAHLMRSLLS RHPALEADKI DDIYWGCVQQ TLEQGFNVAR NAALLAEIPH SVPAVTVNRL CGSSMQALHD AARAIMVGDA GVCLVGGVEH MGHVPMTHGV DFHPGLGKSI AKAAVMMGLT AELLARRHHI SREMQDAFAA RSHQRAWAAT QSGAFRREII PTNGHNADGA LQPFDYDEVV RAETSIDALA ALRPAFDPAN GTVTAGSSSA LSDGAAALLV MSESRALALG LTPRVRIRAM AVVGCDPSVM GYGPVPATHK ALQRAGLSLS DIGLFELNEA FAAQALPCIK ALGLMDSLDD KVNLNGGAIA LGHPLGCSGA RLTATLINLM EQRNVEFGVA TMCIGLGQGI ATVLERV //