DXS_YERP3
ID DXS_YERP3 Reviewed; 619 AA.
AC A7FLE4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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};
GN OrderedLocusNames=YpsIP31758_3112;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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}.
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DR EMBL; CP000720; ABS49260.1; -; Genomic_DNA.
DR RefSeq; WP_012105576.1; NC_009708.1.
DR AlphaFoldDB; A7FLE4; -.
DR SMR; A7FLE4; -.
DR EnsemblBacteria; ABS49260; ABS49260; YpsIP31758_3112.
DR KEGG; ypi:YpsIP31758_3112; -.
DR HOGENOM; CLU_009227_1_4_6; -.
DR OMA; QVGYHAQ; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000002412; Chromosome.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
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: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;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Thiamine biosynthesis;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..619
FT /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT /id="PRO_1000059450"
FT BINDING 80
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 121..123
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 153..154
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 181
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 288
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 370
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ SEQUENCE 619 AA; 67716 MW; 32B554043A7219FC CRC64;
MSLDIAKYPT LALAENPEEL RMLPKESLPK LCDELRQYLL TCVSRSSGHF ASGLGVVELT
VALHYVYNTP FDHLIWDVGH QAYPHKILTG RRDRISTIRQ KDGLHPFPWR GESEYDVLSV
GHSSTSISAG LGMAVAAERE GKGRRTVCVI GDGAITAGMA FEAMSHAGDI HSDMLVILND
NEMSISENVG GLNNHLAQLL SGKLYASLRE GGKKAFSALP PIKDLLKRTE EHLKGMVVPS
TLFEELGFNY IGPVDGHDVH TLTQTLKNMR DLKGPQLLHI MTKKGKGYAP AEKDPIGWHA
VPKFDPASGT LPKSQSSLPT YSKIFGEWLC ETAAKDSKLM AVTPAMREGS GMVRFSREYP
QQYFDVAIAE QHAVTFAAGL AIGGYKPVVA IYSTFLQRAY DQLIHDVAIQ NLPVLFAIDR
GGLVGADGQT HQGAFDLSFM RCIPNMVIMA PSDENECRQM LYTGYHHNGP AAVRYPRGNG
TSAVLEPLEM LPIGKGVLRR EGEKIAILCF GTLLAQAQLA AENLNATLVD MRFVKPLDEE
LVLEMAAKHQ VLVTVEENAI MGGAGSGVNE LLMAKRRWVP VLNIGLPDLF VPQGEQDEMR
SELGLDAAGI QRQIEAWLA
