ID DXS1_ZYMMO Reviewed; 649 AA. AC Q5NN52; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXP synthase 1 {ECO:0000255|HAMAP-Rule:MF_00315}; DE Short=DXPS 1 {ECO:0000255|HAMAP-Rule:MF_00315}; GN Name=dxs1 {ECO:0000255|HAMAP-Rule:MF_00315}; GN OrderedLocusNames=ZMO1234; OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Zymomonadaceae; Zymomonas. OX NCBI_TaxID=264203; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 31821 / ZM4 / CP4; RX PubMed=15592456; DOI=10.1038/nbt1045; RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J., RA Kang H.S.; RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis RT ZM4."; RL Nat. Biotechnol. 23:63-68(2005). 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; 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; AE008692; AAV89858.1; -; Genomic_DNA. DR RefSeq; WP_011241050.1; NZ_CP035711.1. DR AlphaFoldDB; Q5NN52; -. DR SMR; Q5NN52; -. DR STRING; 264203.ZMO1234; -. DR GeneID; 79903641; -. DR KEGG; zmo:ZMO1234; -. DR eggNOG; COG1154; Bacteria. DR HOGENOM; CLU_009227_1_4_5; -. DR UniPathway; UPA00064; UER00091. DR Proteomes; UP000001173; 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; 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. PE 3: Inferred from homology; KW Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome; KW Thiamine biosynthesis; Thiamine pyrophosphate; Transferase. FT CHAIN 1..649 FT /note="1-deoxy-D-xylulose-5-phosphate synthase 1" FT /id="PRO_0000256510" FT BINDING 79 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 120..122 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 151 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 152..153 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 180 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 180 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 289 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" FT BINDING 371 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315" SQ SEQUENCE 649 AA; 70307 MW; 772C535FBA83BE7A CRC64; MFPNDKTPLL DKIKTPAELR QLDRNSLRQL ADELRKETIS AVGVTGGHLG SGLGVIELTV ALHYVFNTPK DALVWDVGHQ TYPHKILTGR RDRIRTLRQR DGLSGFTQRA ESEYDAFGAA HSSTSISAAL GFAMASKLSD SDDKAVAIIG DGSMTAGMAY EAMNNAKAAG KRLIVILNDN EMSISPPVGA LSSYLSRLIS SRPFMNLRDI MRGVVNRMPK GLATAARKAD EYARGMATGG TFFEELGFYY VGPVDGHNLD QLIPVLENVR DAKDGPILVH VVTRKGQGYA PAEAAKDKYH AVQRLDVVSG KQAKAPPGPP SYTSVFSEQL IKEAKQDDKI VTITAAMPTG TGLDRFQQYF PERMFDVGIA EQHAVTFAAG LAAAGYKPFC CLYSTFLQRG YDQLVHDVAI QNLPVRFAVD RAGLVGADGA THAGSFDLAF MVNLPNMVVM APSDERELAN MVHSMAHYDQ GPISVRYPRG NGVGVSLEGE KEILPIGKGR LIRRGKKVAI LSLGTRLEES LKAADRLDAQ GLSTSVADMR FAKPLDEALT RQLLKSHQVI ITIEEGALGG FATQVLTMAS DEGLMDDGLK IRTLRLPDRF QPQDKQERQY AEAGLDADGI VAAVISALHR NSKPVEVVEM ANMGSIARA //