ID THLA_CLOAB Reviewed; 392 AA. AC P45359; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 20-JAN-2009, entry version 66. DE RecName: Full=Acetyl-CoA acetyltransferase; DE EC=2.3.1.9; DE AltName: Full=Acetoacetyl-CoA thiolase; GN Name=thlA; Synonyms=thl; OrderedLocusNames=CA_C2873; OS Clostridium acetobutylicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1488; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX MEDLINE=95172408; PubMed=7867955; DOI=10.1016/0378-1119(94)00838-J; RA Stim-Herndon K.P., Petersen D.J., Bennett G.N.; RT "Characterization of an acetyl-CoA C-acetyltransferase (thiolase) gene RT from Clostridium acetobutylicum ATCC 824."; RL Gene 154:81-85(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX MEDLINE=20525187; PubMed=11075929; RA Winzer K., Lorenz K., Zickner B., Duerre P.; RT "Differential regulation of two thiolase genes from Clostridium RT acetobutylicum DSM 792."; RL J. Mol. Microbiol. Biotechnol. 2:531-541(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX MEDLINE=21359325; PubMed=11466286; RX DOI=10.1128/JB.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., RA Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., RA Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., RA Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). RN [4] RP PROTEIN SEQUENCE OF 1-30. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX MEDLINE=92117621; PubMed=1685080; RA Petersen D.J., Bennett G.N.; RT "Cloning of the Clostridium acetobutylicum ATCC 824 acetyl coenzyme A RT acetyltransferase (thiolase; EC 2.3.1.9) gene."; RL Appl. Environ. Microbiol. 57:2735-2741(1991). CC -!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA. CC -!- PATHWAY: Metabolic intermediate biosynthesis; mevalonic acid CC biosynthesis; (R)-mevalonic acid from acetyl-CoA: step 1/3. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the thiolase family. 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; U08465; AAA82724.1; -; Genomic_DNA. DR EMBL; AF072734; AAC26023.1; -; Genomic_DNA. DR EMBL; AE001437; AAK80816.1; -; Genomic_DNA. DR PIR; E97253; E97253. DR PIR; JC4032; JC4032. DR RefSeq; NP_349476.1; -. DR HSSP; P07097; 1M3K. DR GeneID; 1119056; -. DR GenomeReviews; AE001437_GR; CA_C2873. DR KEGG; cac:CAC2873; -. DR NMPDR; fig|272562.1.peg.3005; -. DR HOGENOM; P45359; -. DR BioCyc; CACE272562:CAC2873-MON; -. DR BioCyc; MetaCyc:THLCLOS-MON; -. DR BRENDA; 2.3.1.9; 2866. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:EC. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR InterPro; IPR002155; Thiolase. DR InterPro; IPR016038; Thiolase-like_subgr. DR Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 1. DR PANTHER; PTHR18919; Thiolase; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. DR PROSITE; PS00099; THIOLASE_3; 1. PE 1: Evidence at protein level; KW Acyltransferase; Complete proteome; Cytoplasm; KW Direct protein sequencing; Transferase. FT CHAIN 1 392 Acetyl-CoA acetyltransferase. FT /FTId=PRO_0000206403. FT ACT_SITE 88 88 Acyl-thioester intermediate (By FT similarity). FT ACT_SITE 348 348 Proton acceptor (By similarity). FT ACT_SITE 378 378 Proton acceptor (By similarity). SQ SEQUENCE 392 AA; 41241 MW; 024D9B21D200856D CRC64; MKEVVIASAV RTAIGSYGKS LKDVPAVDLG ATAIKEAVKK AGIKPEDVNE VILGNVLQAG LGQNPARQAS FKAGLPVEIP AMTINKVCGS GLRTVSLAAQ IIKAGDADVI IAGGMENMSR APYLANNARW GYRMGNAKFV DEMITDGLWD AFNDYHMGIT AENIAERWNI SREEQDEFAL ASQKKAEEAI KSGQFKDEIV PVVIKGRKGE TVVDTDEHPR FGSTIEGLAK LKPAFKKDGT VTAGNASGLN DCAAVLVIMS AEKAKELGVK PLAKIVSYGS AGVDPAIMGY GPFYATKAAI EKAGWTVDEL DLIESNEAFA AQSLAVAKDL KFDMNKVNVN GGAIALGHPI GASGARILVT LVHAMQKRDA KKGLATLCIG GGQGTAILLE KC //