ID THIL_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-1995 (REL. 32, LAST ANNOTATION UPDATE) DE ACETYL-COA ACETYLTRANSFERASE (EC 2.3.1.9) (ACETOACETYL-COA THIOLASE). GN THL. OS CLOSTRIDIUM ACETOBUTYLICUM. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. 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.; RL GENE 154:81-85(1995). RN [2] RP SEQUENCE OF 1-30. RC STRAIN=ATCC 824; RA PETERSEN D.J., BENNETT G.N.; 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 -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SUBUNIT: HOMOTETRAMER. 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; U08465. DR PROSITE; PS00098; THIOLASE_1. DR PROSITE; PS00099; THIOLASE_3. DR PROSITE; PS00737; THIOLASE_2. 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; 721109 CN; 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 //