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 24-JAN-2006 (Rel. 49, Last annotation update) DE Acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase). GN Name=thlA; Synonyms=thl; OrderedLocusNames=CAC2873; 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 / 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 / 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 / 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 / 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; mevalonate CC biosynthesis; R-mevalonate from acetyl-CoA: step 1. CC -!- PATHWAY: Context: Acids (acetate or butyrate) or solvents CC (acetone, butanol or ethanol) biosynthesis. 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; AE007785; AAK80816.1; -; Genomic_DNA. DR PIR; E97253; E97253. DR PIR; JC4032; JC4032. DR HSSP; P07097; 1M3K. DR InterPro; IPR002155; Thiolase. DR PANTHER; PTHR18919; Thiolase; 2. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 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. KW Acyltransferase; Complete proteome; Direct protein sequencing; KW Transferase. 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 //