(data stored in ACNUC7421 zone)

SWISSPROT: DXS_SALTY

ID   DXS_SALTY               Reviewed;         620 AA.
AC   Q8ZRD1;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 109.
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}; OrderedLocusNames=STM0422;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19376.1; -; Genomic_DNA.
DR   RefSeq; NP_459417.1; NC_003197.2.
DR   RefSeq; WP_000006777.1; NC_003197.2.
DR   SMR; Q8ZRD1; -.
DR   PaxDb; Q8ZRD1; -.
DR   PRIDE; Q8ZRD1; -.
DR   EnsemblBacteria; AAL19376; AAL19376; STM0422.
DR   GeneID; 1251941; -.
DR   KEGG; stm:STM0422; -.
DR   PATRIC; fig|99287.12.peg.451; -.
DR   eggNOG; ENOG4105C2V; Bacteria.
DR   eggNOG; COG1154; LUCA.
DR   HOGENOM; HOG000012988; -.
DR   KO; K01662; -.
DR   OMA; QVGYHAQ; -.
DR   PhylomeDB; Q8ZRD1; -.
DR   BioCyc; SENT99287:STM0422-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000001014; 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; Q8ZRD1.
DR   SWISS-2DPAGE; Q8ZRD1.
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..620
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT                   /id="PRO_0000189151"
FT   REGION          121..123
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   REGION          153..154
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   METAL           152
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   METAL           181
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         80
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         181
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         288
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         370
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   620 AA;  67468 MW;  C04D3FCFEDA798CC CRC64;
     MSFDIAKYPT LALVDSTQEL RLLPKESLPK LCDELRRYLL DSVSRSSGHF ASGLGTVELT
     VALHYVYNTP FDQLIWDVGH QAYPHKILTG RRDKIGTIRQ KGGLHPFPWR GESEYDVLSV
     GHSSTSISAG IGIAVAAEKE GKDRRTVCVI GDGAITAGMA FEAMNHAGDI RPDMLVILND
     NEMSISENVG ALNNHLAQLL SGKLYSSLRE GGKKVFSGVP PIKELLKRTE EHIKGMVVPG
     TLFEELGFNY IGPVDGHDVM GLISTLKNMR DLKGPQFLHI MTKKGRGYEP AEKDPITFHA
     VPKFDPSSGC LPKSSGGLPG YSKIFGDWLC ETAAKDSKLM AITPAMREGS GMVEFSRKFP
     DRYFDVAIAE QHAVTFAAGL AIGGYKPVVA IYSTFLQRAY DQVIHDVAIQ KLPVMFAIDR
     AGIVGADGQT HQGAFDLSYL RCIPDMVIMT PSDENECRQM LFTGYHYNDG PTAVRYPRGN
     AQGVALTPLE KLPIGKGLVK RHGEKLAILN FGTLMPEAAK VAEALNATLV DMRFVKPLDD
     TLILEMAAQH DALVTLEENA IMGGAGSGVN EVLMAHRKPV PVLNIGLPDF FIPQGTQEEA
     RAELGLDAAG IEAKIKAWLA
//

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