ID C1B486_RHOOB Unreviewed; 665 AA. AC C1B486; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315}; DE EC=2.2.1.7 {ECO:0000256|HAMAP-Rule:MF_00315}; DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315}; DE Short=DXP synthase {ECO:0000256|HAMAP-Rule:MF_00315}; DE Short=DXPS {ECO:0000256|HAMAP-Rule:MF_00315}; GN Name=dxs {ECO:0000256|HAMAP-Rule:MF_00315, GN ECO:0000313|EMBL:BAH55075.1}; GN OrderedLocusNames=ROP_68280 {ECO:0000313|EMBL:BAH55075.1}; OS Rhodococcus opacus (strain B4). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae; OC Rhodococcus. OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH55075.1, ECO:0000313|Proteomes:UP000002212}; RN [1] {ECO:0000313|EMBL:BAH55075.1, ECO:0000313|Proteomes:UP000002212} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4 {ECO:0000313|EMBL:BAH55075.1, RC ECO:0000313|Proteomes:UP000002212}; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus erythropolis RT PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2009) 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:0000256|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:0000256|HAMAP- CC Rule:MF_00315}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00315}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00315}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00315}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|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. CC {ECO:0000256|ARBA:ARBA00004980, ECO:0000256|HAMAP-Rule:MF_00315}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_00315}. CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily. CC {ECO:0000256|ARBA:ARBA00011081, ECO:0000256|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; AP011115; BAH55075.1; -; Genomic_DNA. DR AlphaFoldDB; C1B486; -. DR STRING; 632772.ROP_68280; -. DR KEGG; rop:ROP_68280; -. DR PATRIC; fig|632772.20.peg.7117; -. DR HOGENOM; CLU_009227_1_4_11; -. DR UniPathway; UPA00064; UER00091. DR Proteomes; UP000002212; 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 CDD; cd07033; TPP_PYR_DXS_TK_like; 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 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 {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP- KW Rule:MF_00315}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00315}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00315}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP- KW Rule:MF_00315}; KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP- KW Rule:MF_00315}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00315}. FT DOMAIN 332..496 FT /note="Transketolase-like pyrimidine-binding" FT /evidence="ECO:0000259|SMART:SM00861" FT BINDING 89 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" FT BINDING 130..132 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" FT BINDING 161 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" FT BINDING 162..163 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" FT BINDING 191 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" FT BINDING 302 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" FT BINDING 383 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315" SQ SEQUENCE 665 AA; 69831 MW; E0A94A32A2152E0E CRC64; MAEARKAACI TEGAISLGVL ARIQTPDDLR QLNPAEMKQL AAEIREFLVQ KVAATGGHLG PNLGVVELTL ALHRIFESPA DPIVFDTGHQ AYVHKILTGR KDDFDSLRKQ GGLSGYPCRA ESDHDWVESS HASAALSYAD GLAKAFELTG QARHVVAVVG DGALTGGMCW EALNNIAAGK DRSVVIVVND NGRSYAPTIG GLADHLAALR LQPGYERILD SGRRMVKKLP WVGRTAYSVL HGMKAGLKDA VAPQVMFTDL GIKYLGPVDG HDEAALESAL RRAKAFGGPV IVHAVTRKGM GYAPAENHVA DQMHSTGVID PVTGKSAGSA SADWTSVFSA ELIDQASHRQ DIVAITAAMA GPTGLAAFGE KYPDRMFDVG IAEQHAVTSA AGLALGGLHP VVAVYSTFLN RAFDQLLMDV ALLKLPVTLV LDRAGITGSD GASHNGMWDM SLLGIVPGMR VAAPRDTATL REELAEALAV DDGPTALRFP KGTVGDDVPA VSRLDGVVDI LHAPSGRNDV LIVSVGAFAG LALAAAERLE QQGISATVVD PRWVLPVPES LLKLAEDSTM VVTVEDSGLH GGVGSTVSAA LRAAGVDVPC RDLGVPQRFL DHASRAQIHA ELGLTAQDVA RQITGWFAGL GNLRPGQQNG VVADLDAQRA ENRGQ //