FADA4_MYCLE
ID FADA4_MYCLE Reviewed; 393 AA.
AC P46707;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Probable acetyl-CoA acetyltransferase;
DE EC=2.3.1.9;
DE AltName: Full=Acetoacetyl-CoA thiolase;
GN Name=fadA4; OrderedLocusNames=ML1158; ORFNames=B1549_C1_166;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U00014; AAA50881.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31539.1; -; Genomic_DNA.
DR PIR; S72804; S72804.
DR RefSeq; NP_301848.1; NC_002677.1.
DR RefSeq; WP_010908172.1; NC_002677.1.
DR AlphaFoldDB; P46707; -.
DR SMR; P46707; -.
DR STRING; 272631.ML1158; -.
DR PRIDE; P46707; -.
DR EnsemblBacteria; CAC31539; CAC31539; CAC31539.
DR KEGG; mle:ML1158; -.
DR PATRIC; fig|272631.5.peg.2090; -.
DR Leproma; ML1158; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_11; -.
DR OMA; ICPSIAI; -.
DR Proteomes; UP000000806; 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; Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Probable acetyl-CoA acetyltransferase"
FT /id="PRO_0000206457"
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 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ SEQUENCE 393 AA; 40529 MW; 9055A3BC878D47E1 CRC64;
MTTSVIVTGA RTPIGKLMGS LKDFSASDLG AITIAAALKK ANVAPSIVQY VIIGQVLTAG
AGQMPARQAA VAAGIGWDVP ALTINKMCLS GLDAIALADQ LIRAGEFDVV VAGGQESMTK
APHLLMDSRS GYKYGDVTIV DHLAYDGLHD VFTNQPMGAL TEQRNDVEKF TRQEQDEFAA
RSHQKAAAAW KDGVFADEVV PVSIPQSKGD SLQFTEDEGI RANTSAESLA GLKPAFRCGG
TITPGSASQI SDGAATVVVM NKEKAQQLGL TWLVEIGAHG VVAGPDSTLQ SQPANAIKKA
VDREGISVEQ LDVVEINEAF AAVALASARE LGIAPELVNV NGGAIAVGHP LGMSGARITL
HVALELARRG SGYGVAALCG AGGQGDALIL RAV