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FADA4_MYCTO
ID   FADA4_MYCTO             Reviewed;         389 AA.
AC   P9WG68; L0T6A9; P66926; Q10629;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   Name=fadA4; OrderedLocusNames=MT1365;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45628.1; -; Genomic_DNA.
DR   PIR; G70769; G70769.
DR   AlphaFoldDB; P9WG68; -.
DR   SMR; P9WG68; -.
DR   EnsemblBacteria; AAK45628; AAK45628; MT1365.
DR   KEGG; mtc:MT1365; -.
DR   PATRIC; fig|83331.31.peg.1472; -.
DR   HOGENOM; CLU_031026_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
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; Transferase.
FT   CHAIN           1..389
FT                   /note="Probable acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000428414"
FT   ACT_SITE        84
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        345
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   389 AA;  40081 MW;  32F892A90364AB05 CRC64;
     MIVAGARTPI GKLMGSLKDF SASELGAIAI KGALEKANVP ASLVEYVIMG QVLTAGAGQM
     PARQAAVAAG IGWDVPALTI NKMCLSGIDA IALADQLIRA REFDVVVAGG QESMTKAPHL
     LMNSRSGYKY GDVTVLDHMA YDGLHDVFTD QPMGALTEQR NDVDMFTRSE QDEYAAASHQ
     KAAAAWKDGV FADEVIPVNI PQRTGDPLQF TEDEGIRANT TAAALAGLKP AFRGDGTITA
     GSASQISDGA AAVVVMNQEK AQELGLTWLA EIGAHGVVAG PDSTLQSQPA NAINKALDRE
     GISVDQLDVV EINEAFAAVA LASIRELGLN PQIVNVNGGA IAVGHPLGMS GTRITLHAAL
     QLARRGSGVG VAALCGAGGQ GDALILRAG
 
 
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