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