(data stored in SCRATCH zone)

SWISSPROT: THL_BACSU

ID   THL_BACSU               Reviewed;         393 AA.
AC   P45855;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   11-DEC-2019, entry version 134.
DE   RecName: Full=Acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   Name=mmgA; Synonyms=yqiL; OrderedLocusNames=BSU24170;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=168 / MB24;
RX   PubMed=8759838; DOI=10.1128/jb.178.16.4778-4786.1996;
RA   Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "A sigma E dependent operon subject to catabolite repression during
RT   sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 178:4778-4786(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
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).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the mother cell at intermediate
CC       stages of sporulation under the control of the sigma-E factor.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- INDUCTION: Subject to catabolite repression.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
DR   EMBL; U29084; AAB09613.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12587.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14348.1; -; Genomic_DNA.
DR   PIR; B69658; B69658.
DR   RefSeq; NP_390297.1; NC_000964.3.
DR   RefSeq; WP_003230291.1; NZ_JNCM01000036.1.
DR   PDB; 5LP7; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-393.
DR   PDBsum; 5LP7; -.
DR   SMR; P45855; -.
DR   STRING; 224308.BSU24170; -.
DR   PaxDb; P45855; -.
DR   PRIDE; P45855; -.
DR   EnsemblBacteria; CAB14348; CAB14348; BSU24170.
DR   GeneID; 938662; -.
DR   KEGG; bsu:BSU24170; -.
DR   PATRIC; fig|224308.179.peg.2631; -.
DR   eggNOG; COG0183; LUCA.
DR   HOGENOM; HOG000012238; -.
DR   InParanoid; P45855; -.
DR   KO; K00626; -.
DR   OMA; LMAGQGQ; -.
DR   PhylomeDB; P45855; -.
DR   BioCyc; BSUB:BSU24170-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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;
DR   PRODOM; P45855.
DR   SWISS-2DPAGE; P45855.
KW   3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Sporulation;
KW   Transferase.
FT   CHAIN           1..393
FT                   /note="Acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000206402"
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"
FT   CONFLICT        68
FT                   /note="Q -> L (in Ref. 1; AAB09613)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..11
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   TURN            20..23
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           26..41
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           45..47
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          51..54
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           65..72
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          81..85
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           90..103
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          108..117
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           118..120
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          123..125
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   TURN            126..130
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          137..141
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           142..146
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   TURN            151..153
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           157..167
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           172..191
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   TURN            192..198
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           207..209
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           226..230
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          234..239
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   TURN            244..246
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          251..261
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           262..267
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          273..283
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           291..303
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           308..310
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          312..316
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           321..331
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           335..337
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           344..347
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   TURN            351..353
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   HELIX           354..368
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          373..380
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   TURN            381..383
FT                   /evidence="ECO:0000244|PDB:5LP7"
FT   STRAND          384..392
FT                   /evidence="ECO:0000244|PDB:5LP7"
SQ   SEQUENCE   393 AA;  41179 MW;  E2D52259679E50F7 CRC64;
     MRKTVIVSAA RTPFGKFGGV LKEVKAAELG GIVMKEALQQ AGVSGDDVEG NVMGMVVQAG
     SGQIPSRQAA RLAGMPWSVP SETLNKVCAS GLRAVTLCDQ MIRAQDADIL VAGGMESMSN
     IPYAVPAGRW GARMGDGELR DLMVYDGLTC AFDEVHMAVH GNTAAKEYAI SRREQDEWAL
     RSHARAAKAA DEGKFQDEIV PVNWIGRKGK PNVVDKDEAI RRDTSLDQLA KLAPIYASDG
     SITAGNAPGV NDGAGAFVLM SEEKAAELGK RPLATILGFS TTGMPAHELA AAPGFAINKL
     LKKNGLTVQD IDLFEVNEAF ASVVLTCEKI VGFDLEKVNV NGGAIALGHP IGASGARILM
     TLVYELKRRG GGLGVAAICS GAAQGDAVLV QVH
//

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