(data stored in SCRATCH zone)

SWISSPROT: DXS_BACSU

ID   DXS_BACSU               Reviewed;         633 AA.
AC   P54523;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 134.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315}; Synonyms=yqiE;
GN   OrderedLocusNames=BSU24270;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
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   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC       and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC       xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC         xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:59776; EC=2.2.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00315};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC       phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
DR   EMBL; D84432; BAA12576.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14358.1; -; Genomic_DNA.
DR   PIR; B69961; B69961.
DR   RefSeq; NP_390307.1; NC_000964.3.
DR   RefSeq; WP_003245985.1; NZ_JNCM01000036.1.
DR   SMR; P54523; -.
DR   STRING; 224308.BSU24270; -.
DR   PaxDb; P54523; -.
DR   PRIDE; P54523; -.
DR   EnsemblBacteria; CAB14358; CAB14358; BSU24270.
DR   GeneID; 938609; -.
DR   KEGG; bsu:BSU24270; -.
DR   PATRIC; fig|224308.179.peg.2645; -.
DR   eggNOG; COG1154; LUCA.
DR   HOGENOM; HOG000012986; -.
DR   InParanoid; P54523; -.
DR   KO; K01662; -.
DR   OMA; QVGYHAQ; -.
DR   PhylomeDB; P54523; -.
DR   BioCyc; BSUB:BSU24270-MONOMER; -.
DR   BioCyc; MetaCyc:BSU24270-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02007; TPP_DXS; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43322; PTHR43322; 1.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; P54523.
DR   SWISS-2DPAGE; P54523.
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..633
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT                   /id="PRO_0000189086"
FT   REGION          113..115
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   REGION          145..146
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   METAL           144
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   METAL           173
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         72
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         173
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         284
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         367
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   633 AA;  69559 MW;  333B65355F0CEF8F CRC64;
     MDLLSIQDPS FLKNMSIDEL EKLSDEIRQF LITSLSASGG HIGPNLGVVE LTVALHKEFN
     SPKDKFLWDV GHQSYVHKLL TGRGKEFATL RQYKGLCGFP KRSESEHDVW ETGHSSTSLS
     GAMGMAAARD IKGTDEYIIP IIGDGALTGG MALEALNHIG DEKKDMIVIL NDNEMSIAPN
     VGAIHSMLGR LRTAGKYQWV KDELEYLFKK IPAVGGKLAA TAERVKDSLK YMLVSGMFFE
     ELGFTYLGPV DGHSYHELIE NLQYAKKTKG PVLLHVITKK GKGYKPAETD TIGTWHGTGP
     YKINTGDFVK PKAAAPSWSG LVSGTVQRMA REDGRIVAIT PAMPVGSKLE GFAKEFPDRM
     FDVGIAEQHA ATMAAAMAMQ GMKPFLAIYS TFLQRAYDQV VHDICRQNAN VFIGIDRAGL
     VGADGETHQG VFDIAFMRHI PNMVLMMPKD ENEGQHMVHT ALSYDEGPIA MRFPRGNGLG
     VKMDEQLKTI PIGTWEVLRP GNDAVILTFG TTIEMAIEAA EELQKEGLSV RVVNARFIKP
     IDEKMMKSIL KEGLPILTIE EAVLEGGFGS SILEFAHDQG EYHTPIDRMG IPDRFIEHGS
     VTALLEEIGL TKQQVANRIR LLMPPKTHKG IGS
//

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