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 02-DEC-2020, entry version 131. 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 5710 OS / 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 from RT 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., Gibson R., RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., RA 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; DOI=10.1128/aem.57.9.2735-2741.1991; 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; Xref=Rhea:RHEA:21036, CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; CC Evidence={ECO:0000255|PROSITE-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 family. CC {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 EnsemblBacteria; AAK80816; AAK80816; CA_C2873. DR GeneID; 44999361; -. DR KEGG; cac:CA_C2873; -. DR PATRIC; fig|272562.8.peg.3057; -. DR eggNOG; COG0183; Bacteria. DR HOGENOM; CLU_031026_0_0_9; -. DR OMA; ICPSIAI; -. 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; Cytoplasm; Direct protein sequencing; KW Reference proteome; Transferase. FT CHAIN 1..392 FT /note="Acetyl-CoA acetyltransferase" FT /id="PRO_0000206403" FT ACT_SITE 88 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 348 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020" FT ACT_SITE 378 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020" FT STRAND 4..11 FT /evidence="ECO:0000244|PDB:4XL2" FT TURN 20..23 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 26..41 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 45..47 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 50..54 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 65..72 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 81..85 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 87..89 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 90..103 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 108..118 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 123..125 FT /evidence="ECO:0000244|PDB:4XL2" FT TURN 126..130 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 142..147 FT /evidence="ECO:0000244|PDB:4XL2" FT TURN 151..154 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 157..168 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 172..191 FT /evidence="ECO:0000244|PDB:4XL2" FT TURN 192..198 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 202..205 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 210..213 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 225..229 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 233..236 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 242..246 FT /evidence="ECO:0000244|PDB:4WYR" FT STRAND 250..260 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 261..266 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 272..279 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 285..290 FT /evidence="ECO:0000244|PDB:4WYR" FT HELIX 294..302 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 307..309 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 311..315 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 320..330 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 334..336 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 343..346 FT /evidence="ECO:0000244|PDB:4XL2" FT HELIX 350..368 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 372..377 FT /evidence="ECO:0000244|PDB:4XL2" FT TURN 381..383 FT /evidence="ECO:0000244|PDB:4XL2" FT STRAND 385..391 FT /evidence="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 //