ID   THLA_STAA8              Reviewed;         393 AA.
AC   Q2G124;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Probable acetyl-CoA acyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   OrderedLocusNames=SAOUHSC_00336;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD29504.1; -; Genomic_DNA.
DR   RefSeq; WP_000199070.1; NZ_LS483365.1.
DR   RefSeq; YP_498926.1; NC_007795.1.
DR   AlphaFoldDB; Q2G124; -.
DR   SMR; Q2G124; -.
DR   STRING; 1280.SAXN108_0404; -.
DR   EnsemblBacteria; ABD29504; ABD29504; SAOUHSC_00336.
DR   GeneID; 3919601; -.
DR   KEGG; sao:SAOUHSC_00336; -.
DR   PATRIC; fig|93061.5.peg.307; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_0_0_9; -.
DR   OMA; ICPSIAI; -.
DR   PRO; PR:Q2G124; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..393
FT                   /note="Probable acetyl-CoA acyltransferase"
FT                   /id="PRO_0000270501"
FT   ACT_SITE        88
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
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"
SQ   SEQUENCE   393 AA;  41704 MW;  9CDF7DB6DF0F6115 CRC64;
     MTRVVLAAAY RTPIGVFGGA FKDVPAYDLG ATLIEHIIKE TGLNPSEIDE VIIGNVLQAG
     QGQNPARIAA MKGGLPETVP AFTVNKVCGS GLKSIQLAYQ SIVTGENDIV LAGGMENMSQ
     SPMLVNNSRF GFKMGHQSMV DSMVYDGLTD VFNQYHMGIT AENLVEQYGI SREEQDTFAV
     NSQQKAVRAQ QNGEFDSEIV PVSIPQRKGE PIVVTKDEGV RENVSVEKLS RLRPAFKKDG
     TVTAGNASGI NDGAAMMLVM SEDKAKELNI EPLAVLDGFG SHGVDPSIMG IAPVGAVEKA
     LKRSKKELSD IDVFELNEAF AAQSLAVDRE LKLPPEKVNV KGGAIALGHP IGASGARVLV
     TLLHQLNDEV ETGLTSLCIG GGQAIAAVVS KYK