ID DXS_COREF Reviewed; 636 AA. AC Q8FPI2; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 28-JAN-2026, entry version 121. 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=CE1796; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). 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 + pyruvate + H(+) = 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; Evidence={ECO:0000255|HAMAP- CC 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; BA000035; BAC18606.1; -; Genomic_DNA. DR RefSeq; WP_006767793.1; NC_004369.1. DR AlphaFoldDB; Q8FPI2; -. DR SMR; Q8FPI2; -. DR STRING; 196164.gene:10742224; -. DR KEGG; cef:CE1796; -. DR eggNOG; COG1154; Bacteria. DR HOGENOM; CLU_009227_1_4_11; -. DR OrthoDB; 9803371at2; -. DR UniPathway; UPA00064; UER00091. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:TreeGrafter. 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 CDD; cd07033; TPP_PYR_DXS_TK_like; 1. DR FunFam; 3.40.50.970:FF:000005; 1-deoxy-D-xylulose-5-phosphate synthase; 1. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 2. 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; IPR049557; Transketolase_CS. DR NCBIfam; TIGR00204; dxs; 1. DR NCBIfam; NF003933; PRK05444.2-2; 1. DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1. DR PANTHER; PTHR43322:SF5; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC; 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; Thiamin diphosphate-binding fold (THDP-binding); 2. DR SUPFAM; SSF52922; TK C-terminal domain-like; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. DR PROSITE; PS00802; TRANSKETOLASE_2; 1. PE 3: Inferred from homology; KW Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Thiamine pyrophosphate; Transferase. FT CHAIN 1..636 FT /note="1-deoxy-D-xylulose-5-phosphate synthase" FT /id="PRO_0000189108" FT BINDING 73 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 114..116 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 146 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 147..148 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 368 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" SQ SEQUENCE 636 AA; 67603 MW; 87298D2324BA184B CRC64; MGILNSISTP ADLKALAEED LEVLAGEIRS FLVDKVAATG GHLGPNLGVV ELTIGLHRVF DSPREPIIFD TSHQSYVHKI LTGRGDAFDT LRQKGGLSGY TSRAESEHDW TESSHASAAL SYADGMSKAF QLDGDTNRNV VAVVGDGALT GGMCWEALNN IAAGKDRNVV VVVNDNGRSY SPTIGGFAEN LAQLRMEPFY DRVMEQGKST LKSMGWVGER TFEALHAFKE GVKSTVIPTE MFPELGMKYI GPVNGHDQKA VDNALAYARD FKGPIIVHVV TEKGRGYAPA ERDLDELMHA TGVMDPRTGI PVAASKPGWT AAFSEELVKL GGRREDIVAI TAAMAGPTGL AKFAANFPSR FYDVGIAEQH ALTSAAGLAL AGKHPVVAIY STFLNRAFDQ LLMDVALLNL PVTVVLDRSG VTGSDGASHN GVWDLALTSI VPGIRVAAPR DEDTLRELLG EAVDINDGPS VVRFPKGDLP APIEAIETLE DGVDILAYLE ASPASEDAPD LLIVAVGERA TLALELGERL VAAGANVTVV DPRWVIPIPQ SLVALAADHD LVITIEDGVI HGGVGSLLSD ALNAAEVDTP RRQVAVPQKF LDHASRGQVL LDHDLDIDSV EKTALGWMDR LFGGGN //