DXS_TREPS
ID DXS_TREPS Reviewed; 630 AA.
AC B2S462;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=TPASS_0824;
OS Treponema pallidum subsp. pallidum (strain SS14).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=455434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS14;
RX PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA Molla M.N., Albert T.J., Weinstock G.M.;
RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT determined with oligonucleotide arrays.";
RL BMC Microbiol. 8:76-76(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000805; ACD71241.1; -; Genomic_DNA.
DR RefSeq; WP_010882268.1; NC_021508.1.
DR AlphaFoldDB; B2S462; -.
DR SMR; B2S462; -.
DR EnsemblBacteria; ACD71241; ACD71241; TPASS_0824.
DR GeneID; 57879341; -.
DR KEGG; tpp:TPASS_0824; -.
DR PATRIC; fig|455434.6.peg.813; -.
DR OMA; QVGYHAQ; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000001202; 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 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; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00204; dxs; 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..630
FT /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT /id="PRO_1000115778"
FT BINDING 75
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 116..118
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 148..149
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 176
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 287
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 367
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ SEQUENCE 630 AA; 68103 MW; 70F4E3340E682448 CRC64;
MDLSLLRSLT GPHDLKSLSP EQVRALAQEV RQEILRVVSA NGGHLASNLG VVELTIALHR
VFSCPHDVVV WDVGHQCYAH KLLTGRAGRF HTLRQKDGIS GFPRRDESPY DAFGTGHSST
ALSAASGILS ALRYRGKSGK VVAVVGDGAL TAGLAFEALL NVGRSCSDLI VILNDNKMSI
SPNTGSFSRY LSTLTVKGPY QKLKTRLRRA LQTVPLVGRP ACRALSRLKR SARTLLYQSN
IFADFGFEYV GPLNGHHIED LERVLNDAKK LTRPTLLHVQ TVKGKGYPFA EQNPTDFHGV
GPFNLAEGIV EKKDALTFTE AFSHTLLNAA RTDDRVVAIT AAMTGGTGLG LFSHIYPERF
FDVGIAEQHA VTFAAGLACA GVKPVVAVYS TFLQRAVDQV IHDVAVQNLP VIFALDRAGA
VPHDGETHQG LFDLSILRAV PNINILCPAS AHELSLLFGW ALAQDTPVAI RYPKALCPPE
EDGFSTPVHT GRGVLITREN ECNVLLVCTG GVFPEVTAAA NTLARKGIFA DIYNVRFVKP
VDEDYFLDLV GRYRSVLFVE DGVKIGGIAE ALQALLNTRH PAPCSDVLAF QDMFYPHGSR
AQVLAAAGLS APHIAARAEW LLAHSVGQIR
