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 08-MAY-2019, entry version 125. 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 (strain ATCC 824 / DSM 792 / JCM 1419 / LMG OS 5710 / VKM B-1787). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787; RX 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 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 PubMed=11466286; 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 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: CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; CC Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10020}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase CC family. {ECO:0000305}. 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; NC_003030.1. DR RefSeq; WP_010966157.1; NC_003030.1. DR PDB; 4WYR; X-ray; 2.30 A; A/B=1-392. DR PDB; 4XL2; X-ray; 1.77 A; A/B=1-392. DR PDBsum; 4WYR; -. DR PDBsum; 4XL2; -. DR SMR; P45359; -. DR STRING; 272562.CA_C2873; -. DR PRIDE; P45359; -. DR EnsemblBacteria; AAK80816; AAK80816; CA_C2873. DR GeneID; 1119056; -. DR KEGG; cac:CA_C2873; -. DR PATRIC; fig|272562.8.peg.3057; -. DR eggNOG; ENOG4105CHU; Bacteria. DR eggNOG; COG0183; LUCA. DR HOGENOM; HOG000012238; -. DR KO; K00626; -. DR OMA; WDVYNKF; -. DR OrthoDB; 1058688at2; -. DR BioCyc; MetaCyc:THLCLOS-MONOMER; -. DR SABIO-RK; P45359; -. DR UniPathway; UPA00058; UER00101. DR Proteomes; UP000000814; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC. DR CDD; cd00751; thiolase; 1. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR002155; Thiolase. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS. DR InterPro; IPR020610; Thiolase_AS. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020613; Thiolase_CS. DR InterPro; IPR020616; Thiolase_N. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; SSF53901; 2. 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 3D-structure; Acyltransferase; Complete proteome; Cytoplasm; KW Direct protein sequencing; Reference proteome; Transferase. FT CHAIN 1 392 Acetyl-CoA acetyltransferase. FT /FTId=PRO_0000206403. FT ACT_SITE 88 88 Acyl-thioester intermediate. FT {ECO:0000250}. FT ACT_SITE 348 348 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10020}. FT ACT_SITE 378 378 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10020}. FT STRAND 4 11 {ECO:0000244|PDB:4XL2}. FT TURN 20 23 {ECO:0000244|PDB:4XL2}. FT HELIX 26 41 {ECO:0000244|PDB:4XL2}. FT HELIX 45 47 {ECO:0000244|PDB:4XL2}. FT STRAND 50 54 {ECO:0000244|PDB:4XL2}. FT HELIX 65 72 {ECO:0000244|PDB:4XL2}. FT STRAND 81 85 {ECO:0000244|PDB:4XL2}. FT HELIX 87 89 {ECO:0000244|PDB:4XL2}. FT HELIX 90 103 {ECO:0000244|PDB:4XL2}. FT STRAND 108 118 {ECO:0000244|PDB:4XL2}. FT STRAND 123 125 {ECO:0000244|PDB:4XL2}. FT TURN 126 130 {ECO:0000244|PDB:4XL2}. FT HELIX 142 147 {ECO:0000244|PDB:4XL2}. FT TURN 151 154 {ECO:0000244|PDB:4XL2}. FT HELIX 157 168 {ECO:0000244|PDB:4XL2}. FT HELIX 172 191 {ECO:0000244|PDB:4XL2}. FT TURN 192 198 {ECO:0000244|PDB:4XL2}. FT STRAND 202 205 {ECO:0000244|PDB:4XL2}. FT STRAND 210 213 {ECO:0000244|PDB:4XL2}. FT HELIX 225 229 {ECO:0000244|PDB:4XL2}. FT STRAND 233 236 {ECO:0000244|PDB:4XL2}. FT STRAND 242 246 {ECO:0000244|PDB:4WYR}. FT STRAND 250 260 {ECO:0000244|PDB:4XL2}. FT HELIX 261 266 {ECO:0000244|PDB:4XL2}. FT STRAND 272 279 {ECO:0000244|PDB:4XL2}. FT HELIX 285 290 {ECO:0000244|PDB:4WYR}. FT HELIX 294 302 {ECO:0000244|PDB:4XL2}. FT HELIX 307 309 {ECO:0000244|PDB:4XL2}. FT STRAND 311 315 {ECO:0000244|PDB:4XL2}. FT HELIX 320 330 {ECO:0000244|PDB:4XL2}. FT HELIX 334 336 {ECO:0000244|PDB:4XL2}. FT HELIX 343 346 {ECO:0000244|PDB:4XL2}. FT HELIX 350 368 {ECO:0000244|PDB:4XL2}. FT STRAND 372 377 {ECO:0000244|PDB:4XL2}. FT TURN 381 383 {ECO:0000244|PDB:4XL2}. FT STRAND 385 391 {ECO:0000244|PDB:4XL2}. 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 //