ID DXS_ECOLI Reviewed; 620 AA. AC P77488; Q2MC06; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 10-JUN-2026, entry version 199. DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000303|PubMed:9371765, ECO:0000305|PubMed:9482846}; DE EC=2.2.1.7 {ECO:0000269|PubMed:9371765, ECO:0000269|PubMed:9482846}; DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000303|PubMed:9371765}; DE Short=DXP synthase {ECO:0000303|PubMed:9371765}; DE Short=DXPS; GN Name=dxs {ECO:0000303|PubMed:9482846}; Synonyms=yajP; GN OrderedLocusNames=b0420, JW0410; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=K12; RX PubMed=9482846; DOI=10.1073/pnas.95.5.2105; RA Lois L.M., Campos N., Rosa Putra S., Danielsen K., Rohmer M., Boronat A.; RT "Cloning and characterization of a gene from Escherichia coli encoding a RT transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose RT 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol RT biosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 95:2105-2110(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 2-7, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=9371765; DOI=10.1073/pnas.94.24.12857; RA Sprenger G.A., Schorken U., Wiegert T., Grolle S., de Graaf A.A., RA Taylor S.V., Begley T.P., Bringer-Meyer S., Sahm H.; RT "Identification of a thiamin-dependent synthase in Escherichia coli RT required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor RT to isoprenoids, thiamin, and pyridoxol."; RL Proc. Natl. Acad. Sci. U.S.A. 94:12857-12862(1997). RN [6] RP CHARACTERIZATION. RX PubMed=10648511; DOI=10.1128/jb.182.4.891-897.2000; RA Kuzuyama T., Takagi M., Takahashi S., Seto H.; RT "Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase RT from Streptomyces sp. strain CL190, which uses both the mevalonate and RT nonmevalonate pathways for isopentenyl diphosphate biosynthesis."; RL J. Bacteriol. 182:891-897(2000). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND RP THIAMINE PYROPHOSPHATE, FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF RP GLU-370; TYR-392; ARG-398; HIS-431 AND ARG-478. RX PubMed=17135236; DOI=10.1074/jbc.m610235200; RA Xiang S., Usunow G., Lange G., Busch M., Tong L.; RT "Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial RT enzyme for isoprenoids biosynthesis."; RL J. Biol. Chem. 282:2676-2682(2007). 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:0000269|PubMed:17135236, CC ECO:0000269|PubMed:9371765, ECO:0000269|PubMed:9482846}. 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:0000269|PubMed:9371765, CC ECO:0000269|PubMed:9482846}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12606; CC Evidence={ECO:0000305|PubMed:9371765, ECO:0000305|PubMed:9482846}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:17135236}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17135236}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000269|PubMed:17135236, ECO:0000269|PubMed:9371765}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000269|PubMed:17135236}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5-8.0.; CC Temperature dependence: CC Optimum temperature is 42-44 degrees Celsius.; 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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17135236}. CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily. CC {ECO:0000305}. 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; AF035440; AAC46162.1; -; Genomic_DNA. DR EMBL; U82664; AAB40176.1; -; Genomic_DNA. DR EMBL; U00096; AAC73523.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76200.1; -; Genomic_DNA. DR PIR; D64771; D64771. DR RefSeq; NP_414954.1; NC_000913.3. DR RefSeq; WP_000006797.1; NZ_CP009789.1. DR PDB; 2O1S; X-ray; 2.40 A; A/B/C/D=1-620. DR AlphaFoldDB; P77488; -. DR SMR; P77488; -. DR BioGRID; 4259592; 371. DR DIP; DIP-9485N; -. DR FunCoup; P77488; 673. DR IntAct; P77488; 19. DR MINT; P77488; -. DR STRING; 511145.b0420; -. DR BindingDB; P77488; -. DR ChEMBL; CHEMBL3217381; -. DR jPOST; P77488; -. DR PaxDb; 511145-b0420; -. DR EnsemblBacteria; AAC73523; AAC73523; b0420. DR GeneID; 945060; -. DR KEGG; ecj:JW0410; -. DR KEGG; eco:b0420; -. DR KEGG; ecoc:C3026_02050; -. DR PATRIC; fig|1411691.4.peg.1857; -. DR EchoBASE; EB3378; -. DR eggNOG; COG1154; Bacteria. DR HOGENOM; CLU_009227_1_4_6; -. DR InParanoid; P77488; -. DR OMA; QVGYHAQ; -. DR OrthoDB; 9803371at2; -. DR PhylomeDB; P77488; -. DR BioCyc; EcoCyc:DXS-MONOMER; -. DR BioCyc; MetaCyc:DXS-MONOMER; -. DR BRENDA; 2.2.1.7; 2026. DR SABIO-RK; P77488; -. DR UniPathway; UPA00064; UER00091. DR EvolutionaryTrace; P77488; -. DR PRO; PR:P77488; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P77488; -. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IDA:EcoCyc. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IMP:EcoCyc. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IMP:EcoCyc. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IDA:EcoCyc. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:EcoCyc. DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:EcoCyc. 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: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. DR PDBsum; 2O1S; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Isoprene biosynthesis; Magnesium; KW Metal-binding; Reference proteome; Thiamine biosynthesis; KW Thiamine pyrophosphate; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9371765" FT CHAIN 2..620 FT /note="1-deoxy-D-xylulose-5-phosphate synthase" FT /id="PRO_0000189111" FT BINDING 80 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:17135236" FT BINDING 121..123 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT BINDING 152 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:17135236" FT BINDING 153..154 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:17135236" FT BINDING 181 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:17135236" FT BINDING 288 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:17135236" FT BINDING 370 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000269|PubMed:17135236" FT MUTAGEN 370 FT /note="E->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:17135236" FT MUTAGEN 392 FT /note="Y->A: Slightly increases activity." FT /evidence="ECO:0000269|PubMed:17135236" FT MUTAGEN 392 FT /note="Y->F: Increases activity 3-fold." FT /evidence="ECO:0000269|PubMed:17135236" FT MUTAGEN 398 FT /note="R->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:17135236" FT MUTAGEN 431 FT /note="H->A: No effect on activity." FT /evidence="ECO:0000269|PubMed:17135236" FT MUTAGEN 478 FT /note="R->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:17135236" FT TURN 5..7 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 11..13 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 17..20 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 28..42 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 57..66 FT /evidence="ECO:0007829|PDB:2O1S" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 72..79 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 87..91 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 92..97 FT /evidence="ECO:0007829|PDB:2O1S" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 126..140 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 158..170 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 173..180 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 240..245 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 249..255 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 259..271 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 274..281 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 321..335 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 339..345 FT /evidence="ECO:0007829|PDB:2O1S" FT TURN 347..351 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 353..358 FT /evidence="ECO:0007829|PDB:2O1S" FT TURN 360..362 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 370..382 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 386..392 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 395..399 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 402..408 FT /evidence="ECO:0007829|PDB:2O1S" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 415..420 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 436..439 FT /evidence="ECO:0007829|PDB:2O1S" FT TURN 440..442 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 454..466 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 472..475 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 484..486 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 491..493 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 498..501 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 504..512 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 515..525 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 528..531 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 534..537 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 540..549 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 551..561 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 565..575 FT /evidence="ECO:0007829|PDB:2O1S" FT STRAND 582..587 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 591..594 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 597..603 FT /evidence="ECO:0007829|PDB:2O1S" FT HELIX 608..619 FT /evidence="ECO:0007829|PDB:2O1S" SQ SEQUENCE 620 AA; 67617 MW; EAF8919809CDF6A1 CRC64; MSFDIAKYPT LALVDSTQEL RLLPKESLPK LCDELRRYLL DSVSRSSGHF ASGLGTVELT VALHYVYNTP FDQLIWDVGH QAYPHKILTG RRDKIGTIRQ KGGLHPFPWR GESEYDVLSV GHSSTSISAG IGIAVAAEKE GKNRRTVCVI GDGAITAGMA FEAMNHAGDI RPDMLVILND NEMSISENVG ALNNHLAQLL SGKLYSSLRE GGKKVFSGVP PIKELLKRTE EHIKGMVVPG TLFEELGFNY IGPVDGHDVL GLITTLKNMR DLKGPQFLHI MTKKGRGYEP AEKDPITFHA VPKFDPSSGC LPKSSGGLPS YSKIFGDWLC ETAAKDNKLM AITPAMREGS GMVEFSRKFP DRYFDVAIAE QHAVTFAAGL AIGGYKPIVA IYSTFLQRAY DQVLHDVAIQ KLPVLFAIDR AGIVGADGQT HQGAFDLSYL RCIPEMVIMT PSDENECRQM LYTGYHYNDG PSAVRYPRGN AVGVELTPLE KLPIGKGIVK RRGEKLAILN FGTLMPEAAK VAESLNATLV DMRFVKPLDE ALILEMAASH EALVTVEENA IMGGAGSGVN EVLMAHRKPV PVLNIGLPDF FIPQGTQEEM RAELGLDAAG MEAKIKAWLA //