ID THLA_CLOAB STANDARD; PRT; 392 AA. AC P45359; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase). GN THLA OR THL OR CAC2873. OS Clostridium acetobutylicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1488; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 824 / DSM 792 / VKM B-1787; RX MEDLINE=95172408; PubMed=7867955; RA Stim-Herndon K.P., Petersen D.J., Bennett G.N.; RT "Characterization of an acetyl-CoA C-acetyltransferase (thiolase) RT gene from Clostridium acetobutylicum ATCC 824."; RL Gene 154:81-85(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 824 / DSM 792 / 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 SEQUENCE FROM N.A. RC STRAIN=ATCC 824 / DSM 792 / VKM B-1787; RX MEDLINE=21359325; PubMed=11466286; 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., Soucaille P., Daly M.J., RA 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 SEQUENCE OF 1-30. RC STRAIN=ATCC 824 / DSM 792 / 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: Junction in the pathway leading to the production of CC either acids (acetate or butyrate) or solvents (acetone, butanol CC or ethanol). CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. 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; -. DR EMBL; AF072734; AAC26023.1; -. DR EMBL; AE007785; AAK80816.1; -. DR PIR; E97253; E97253. DR PIR; JC4032; JC4032. DR HSSP; P27796; 1AFY. DR InterPro; IPR002155; Thiolase. DR Pfam; PF00108; thiolase; 1. DR Pfam; PF02803; thiolase_C; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00099; THIOLASE_3; 1. DR PROSITE; PS00737; THIOLASE_2; 1. KW Transferase; Acyltransferase; Complete proteome. FT ACT_SITE 88 88 Substrate binding (By similarity). FT ACT_SITE 378 378 Base (By similarity). SQ SEQUENCE 392 AA; 41240 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 //