ID   FADA_BACSU              Reviewed;         391 AA.
AC   O32177;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=3-ketoacyl-CoA thiolase;
DE            EC=2.3.1.16;
DE   AltName: Full=Acetyl-CoA acyltransferase;
DE   AltName: Full=Beta-ketothiolase;
GN   Name=fadA; Synonyms=yusK; OrderedLocusNames=BSU32830;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [2]
RP   GENE NAME, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=17189250; DOI=10.1074/jbc.m606831200;
RA   Matsuoka H., Hirooka K., Fujita Y.;
RT   "Organization and function of the YsiA regulon of Bacillus subtilis
RT   involved in fatty acid degradation.";
RL   J. Biol. Chem. 282:5180-5194(2007).
CC   -!- FUNCTION: Involved in the degradation of long-chain fatty acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- INDUCTION: Repressed by FadR in the absence of LCFAs (fatty acids of
CC       14-20 carbon atoms). When LCFAs are present in the medium, they are
CC       converted to long-chain acyl-CoAs, which antagonize FadR as to its
CC       binding to fadR boxes on target DNA and thus derepress transcription.
CC       {ECO:0000269|PubMed:17189250}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; AL009126; CAB15272.1; -; Genomic_DNA.
DR   PIR; D70021; D70021.
DR   RefSeq; NP_391162.1; NC_000964.3.
DR   RefSeq; WP_003228574.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32177; -.
DR   SMR; O32177; -.
DR   STRING; 224308.BSU32830; -.
DR   PaxDb; O32177; -.
DR   PRIDE; O32177; -.
DR   EnsemblBacteria; CAB15272; CAB15272; BSU_32830.
DR   GeneID; 936729; -.
DR   KEGG; bsu:BSU32830; -.
DR   PATRIC; fig|224308.179.peg.3557; -.
DR   eggNOG; COG0183; Bacteria.
DR   InParanoid; O32177; -.
DR   OMA; DYYWGMG; -.
DR   PhylomeDB; O32177; -.
DR   BioCyc; BSUB:BSU32830-MON; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IBA:GO_Central.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
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   2: Evidence at transcript level;
KW   Acyltransferase; Fatty acid metabolism; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..391
FT                   /note="3-ketoacyl-CoA thiolase"
FT                   /id="PRO_0000360669"
FT   ACT_SITE        90
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   391 AA;  41123 MW;  B326A3D6A64E5799 CRC64;
     MKEAVIVSGA RTPVGKAKKG SLATVRPDDL GAICVKETLK RAGGYEGNID DLIIGCATPE
     AEQGLNMARN IGALAGLPYT VPAITVNRYC SSGLQSIAYA AEKIMLGAYD TAIAGGAESM
     SQVPMMGHVT RPNLALAEKA PEYYMSMGHT AEQVAKKYGV SREDQDAFAV RSHQNAAKAL
     AEGKFKDEIV PVEVTVTEIG EDHKPMEKQF VFSQDEGVRP QTTADILSTL RPAFSVDGTV
     TAGNSSQTSD GAAAVMLMDR EKADALGLAP LVKFRSFAVG GVPPEVMGIG PVEAIPRALK
     LAGLQLQDIG LFELNEAFAS QAIQVIRELG IDEEKVNVNG GAIALGHPLG CTGTKLTLSL
     IHEMKRRNEQ FGVVTMCIGG GMGAAGVFEL C