ID   FADA4_MYCS2             Reviewed;         388 AA.
AC   A0R1Y7; I7GD60;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   OrderedLocusNames=MSMEG_4920, MSMEI_4793;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-187, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK71664.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AFP41241.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK71664.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001663; AFP41241.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_889175.1; NC_008596.1.
DR   AlphaFoldDB; A0R1Y7; -.
DR   SMR; A0R1Y7; -.
DR   STRING; 246196.MSMEI_4793; -.
DR   PRIDE; A0R1Y7; -.
DR   EnsemblBacteria; ABK71664; ABK71664; MSMEG_4920.
DR   EnsemblBacteria; AFP41241; AFP41241; MSMEI_4793.
DR   KEGG; msg:MSMEI_4793; -.
DR   KEGG; msm:MSMEG_4920; -.
DR   PATRIC; fig|246196.19.peg.4801; -.
DR   eggNOG; COG0183; Bacteria.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   1: Evidence at protein level;
KW   Acyltransferase; Isopeptide bond; Reference proteome; Transferase;
KW   Ubl conjugation.
FT   CHAIN           1..388
FT                   /note="Probable acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000396110"
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"
FT   CROSSLNK        187
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   388 AA;  40067 MW;  0783715F6801E1E0 CRC64;
     MIVAGARTPV GKLMGSLKDF SGTDLGAIAI RAALEKANVP ASMVEYVIMG QVLTAGAGQM
     PARQAAVAAG IPWDVAALSI NKMCLSGIDA IALADQLIRA GEFDVIVAGG QESMSQAPHL
     LPKSREGYKY GDATLVDHLA YDGLHDVFTD QPMGALTEQR NDVDKFTRAE QDEYAAQSHQ
     KAAAAWKDGV FADEVVPVSI PQRKGDPIEF AEDEGIRANT TAESLAGLKP AFRKDGTITA
     GSASQISDGA AAVIVMNKAK AEELGLTWLA EIGAHGVVAG PDSTLQSQPA NAIKKAITRE
     GITVDQLDVI EINEAFAAVA LASTKELGVD PAKVNVNGGA IAIGHPIGMS GARIALHAAL
     ELARRGSGYA VAALCGAGGQ GDALVLRR