THLA_STAES
ID THLA_STAES Reviewed; 394 AA.
AC Q8CQN7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Probable acetyl-CoA acyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
GN OrderedLocusNames=SE_2384;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO06027.1; -; Genomic_DNA.
DR RefSeq; NP_765939.1; NC_004461.1.
DR RefSeq; WP_001831350.1; NZ_WBME01000004.1.
DR AlphaFoldDB; Q8CQN7; -.
DR SMR; Q8CQN7; -.
DR STRING; 176280.SE_2384; -.
DR EnsemblBacteria; AAO06027; AAO06027; SE_2384.
DR GeneID; 50019690; -.
DR KEGG; sep:SE_2384; -.
DR PATRIC; fig|176280.10.peg.2323; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_9; -.
DR OMA; ICPSIAI; -.
DR Proteomes; UP000001411; 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 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..394
FT /note="Probable acetyl-CoA acyltransferase"
FT /id="PRO_0000270510"
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 394 AA; 41595 MW; C95DCBE16F213195 CRC64;
MSRIVLAEAY RTPIGVFGGV FKDIPAYELG ATVIRQILEH SQIDPNEINE VILGNVLQAG
QGQNPARIAA IHGGVPEAVP SFTVNKVCGS GLKAIQLAYQ SIVAGDNEIV IAGGMESMSQ
SPMLLKNSRF GFKMGNQTLE DSMIADGLTD KFNDYHMGIT AENLVEQYQI SRKEQDQFAF
DSQQKASRAQ QAGVFDAEIV PVEVPQRKGD PLIISQDEGI RPQTTIDKLA QLRPAFKKDG
SVTAGNASGI NDGAAAMLVM TEDKAKALGL QPIAVLDSFG ASGVAPSIMG IGPVEAIHKA
LKRSNKVIND VDIFELNEAF AAQSIAVNRE LQLPQDKVNV NGGAIALGHP IGASGARTLV
SLLHQLSDAK PTGVASLCIG GGQGIATVVS KYEV
