ID THL_CLOAB STANDARD; PRT; 392 AA. AC P45359; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE ACETYL-COA ACETYLTRANSFERASE (EC 2.3.1.9) (ACETOACETYL-COA THIOLASE). GN THL. OS Clostridium acetobutylicum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 824; RX MEDLINE; 95172408. 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 OF 1-30. RC STRAIN=ATCC 824; RX MEDLINE; 92117621. 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 This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 HSSP; P27796; 1AFW. DR PFAM; PF00108; thiolase; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00099; THIOLASE_3; 1. DR PROSITE; PS00737; THIOLASE_2; 1. KW Transferase; Acyltransferase. FT ACT_SITE 88 88 SUBSTRATE BINDING (BY SIMILARITY). FT ACT_SITE 378 378 BASE (BY SIMILARITY). SQ SEQUENCE 392 AA; 41240 MW; 1D091D97 CRC32; 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 //