ID DXS_BACC2 Reviewed; 630 AA. AC B7IXG8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 02-SEP-2026, entry version 85. 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=BCG9842_B0947; OS Bacillus cereus (strain G9842). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=405531; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus G9842."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. 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; CP001186; ACK95491.1; -; Genomic_DNA. DR RefSeq; WP_000366457.1; NC_011772.1. DR AlphaFoldDB; B7IXG8; -. DR SMR; B7IXG8; -. DR KEGG; bcg:BCG9842_B0947; -. DR HOGENOM; CLU_009227_1_4_9; -. DR UniPathway; UPA00064; UER00091. 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; 3.40.50.920:FF:000002; 1-deoxy-D-xylulose-5-phosphate synthase; 1. DR FunFam; 3.40.50.970:FF:000030; 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; Thiamine biosynthesis; KW Thiamine pyrophosphate; Transferase. FT CHAIN 1..630 FT /note="1-deoxy-D-xylulose-5-phosphate synthase" FT /id="PRO_1000119538" FT BINDING 72 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 113..115 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 144 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 145..146 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 173 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 173 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 284 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; 69410 MW; A1B6D66D69DACC71 CRC64; MDLTQIQNPS FLKDMSISEL EGLSEDIRKF LIEELSQTGG HIAPNLGVVE LTIALHKLFD SPQDKFLWDV GHQSYVHKIL TGRAKEFGTL RQYQGLCGFP KRCESEHDVW ETGHSSTSLS AAMGMALARD LKKTKEYVIP IIGDGALTGG MALEALNHIG HEKTDMIVIL NDNEMSIAPN VGALHNVLGR LRTAGKYHWV KDELEYILKK IPAVGGKVAA TAEKIKDSLK YLLVSGVFFE ELGFTYLGPV DGHDYEKLFE TLQYAKKTKG PVLVHVITKK GKGYKPAESD VIGTWHGTGP YKIESGDFVK PKEVAPAWSA VVSETVLKLA RADERIVAIT PAMPVGSKLE KFQKEFPNRM IDVGIAEQHA TTMAAGMATQ GMKPFLAIYS TFLQRAYDQV VHDICRQNLN VFIGIDRSGL VGADGETHQG VFDISFLRHL PNMVLMMPKD ENEGQHLVYT AMQYEDGPIA LRYARGNGLG VHMDEELKAI PIGTWETLKE GTQAAILTFG TTIPMAMEAA ERLEKAGVSV KVVNARFIKP MDEAYLHDLL GKNIPILTIE EACLIGGFGT GVVEFASENG YHSALVERMG IPDRFIEHGS VTKLLEEIGL TTDAVVDRIH TMIPSKQKRA //