ID THLA_CLODI Reviewed; 107 AA. AC P45362; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 98. DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000250|UniProtKB:P45359}; DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P45359}; DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000250|UniProtKB:P45359}; DE Flags: Fragment; GN Name=thi; OS Clostridioides difficile (Peptoclostridium difficile). OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales; OC Peptostreptococcaceae; Clostridioides. OX NCBI_TaxID=1496; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=E; RX PubMed=8001771; DOI=10.1111/j.1574-6968.1994.tb07262.x; RA Mullany P., Clayton C.L., Pallen M.J., Slone R., Al-Saleh A., RA Tabaqchali S.; RT "Genes encoding homologues of three consecutive enzymes in the RT butyrate/butanol-producing pathway of Clostridium acetobutylicum are RT clustered on the Clostridium difficile chromosome."; RL FEMS Microbiol. Lett. 124:61-67(1994). CC -!- FUNCTION: Catalyzes the condensation of two molecules of acetyl-CoA to CC produce acetoacetyl-CoA. {ECO:0000250|UniProtKB:P45359}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; CC Evidence={ECO:0000250|UniProtKB:P45359}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P45359}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45359}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA56273.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; X79899; CAA56273.1; ALT_INIT; Genomic_DNA. DR PIR; I40680; I40680. DR AlphaFoldDB; P45362; -. DR SMR; P45362; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISS:UniProtKB. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020616; Thiolase_N. DR PANTHER; PTHR18919:SF107; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 1. DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1. DR Pfam; PF00108; Thiolase_N; 1. DR SUPFAM; SSF53901; Thiolase-like; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Transferase. FT CHAIN 1..>107 FT /note="Acetyl-CoA acetyltransferase" FT /id="PRO_0000206404" FT ACT_SITE 88 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000250|UniProtKB:P45359" FT NON_TER 107 SQ SEQUENCE 107 AA; 11101 MW; CE702BBFB1AF0713 CRC64; MREVVIASAA RTAVGSFGGA FKSVSAVELG VTAAKEAIKR ANITPDMIDE SLLGGVLTAG LGQNIARQIA LGAGIPVEKP AMTINIVCGS GLRSWRALRT RTGPRRR //