ID   THLA_SYNWW              Reviewed;         396 AA.
AC   Q0AVM3;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000303|PubMed:23468890};
DE            EC=2.3.1.9 {ECO:0000305|PubMed:23468890};
DE   AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000303|PubMed:23468890};
GN   OrderedLocusNames=Swol_1934 {ECO:0000312|EMBL:ABI69231.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
RP   FUNCTION, AND PATHWAY.
RX   PubMed=23468890; DOI=10.1371/journal.pone.0056905;
RA   Schmidt A., Mueller N., Schink B., Schleheck D.;
RT   "A proteomic view at the biochemistry of syntrophic butyrate oxidation in
RT   Syntrophomonas wolfei.";
RL   PLoS ONE 8:E56905-E56905(2013).
CC   -!- FUNCTION: Involved in syntrophic growth of S.wolfei with butyrate, as
CC       part of the butyrate oxidation pathway. Probably catalyzes the beta-
CC       keto thiolysis of acetoacetyl-CoA, leading to 2 acetyl-CoA molecules.
CC       {ECO:0000305|PubMed:23468890}.
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:0000305|PubMed:23468890};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000305|PubMed:23468890}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23468890}.
CC   -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at
CC       protein level). Seems to be constitutively expressed.
CC       {ECO:0000269|PubMed:23468890}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000448; ABI69231.1; -; Genomic_DNA.
DR   RefSeq; WP_011641324.1; NC_008346.1.
DR   AlphaFoldDB; Q0AVM3; -.
DR   SMR; Q0AVM3; -.
DR   STRING; 335541.Swol_1934; -.
DR   PRIDE; Q0AVM3; -.
DR   EnsemblBacteria; ABI69231; ABI69231; Swol_1934.
DR   KEGG; swo:Swol_1934; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_0_0_9; -.
DR   OMA; VNQFHGA; -.
DR   OrthoDB; 1058688at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
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   Acyltransferase; Cytoplasm; Fatty acid metabolism; Lipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..396
FT                   /note="Acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000442213"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
FT   ACT_SITE        352
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
FT   ACT_SITE        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
FT   BINDING         223..225
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
FT   BINDING         249
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
SQ   SEQUENCE   396 AA;  41283 MW;  560E0C2E56776DF8 CRC64;
     MTREVVLVGA CRTPVGTFGG TLKDVGSAQL GAIVMGEAIK RAGIKAEQID EVIFGCVLQA
     GLGQNVARQC MINAGIPKEV TAFTINKVCG SGLRAVSLAA QVIKAGDADI IMAGGTENMD
     KAPFILPNAR WGYRMSMPKG DLIDEMVWGG LTDVFNGYHM GITAENINDM YGITREEQDA
     FGFRSQTLAA QAIESGRFKD EIVPVVIKGK KGDIVFDTDE HPRKSTPEAM AKLAPAFKKG
     GSVTAGNASG INDAAAAVIV MSKEKADELG IKPMAKVVSY ASGGVDPSVM GLGPIPASRK
     ALEKAGLTID DIDLIEANEA FAAQSIAVAR DLGWADKMEK VNVNGGAIAI GHPIGSSGAR
     ILVTLLYEMQ KRGSKKGLAT LCIGGGMGTA LIVEAL