THLA_STAEQ
ID THLA_STAEQ Reviewed; 394 AA.
AC Q5HS07;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Probable acetyl-CoA acyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
GN OrderedLocusNames=SERP0032;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53454.1; -; Genomic_DNA.
DR RefSeq; WP_001831350.1; NC_002976.3.
DR AlphaFoldDB; Q5HS07; -.
DR SMR; Q5HS07; -.
DR STRING; 176279.SERP0032; -.
DR EnsemblBacteria; AAW53454; AAW53454; SERP0032.
DR GeneID; 50019690; -.
DR KEGG; ser:SERP0032; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_9; -.
DR OMA; ICPSIAI; -.
DR OrthoDB; 1058688at2; -.
DR Proteomes; UP000000531; 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; Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Probable acetyl-CoA acyltransferase"
FT /id="PRO_0000270509"
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
