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DXS_PSEAE
ID   DXS_PSEAE               Reviewed;         627 AA.
AC   Q9KGU7;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
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=PA4044;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=11034300; DOI=10.1111/j.1574-6968.2000.tb09307.x;
RA   Altincicek B., Hintz M., Sanderbrand S., Wiesner J., Beck E., Jomaa H.;
RT   "Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate
RT   (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the
RT   pathogenic bacterium Pseudomonas aeruginosa.";
RL   FEMS Microbiol. Lett. 190:329-333(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; AF282878; AAF97240.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG07431.1; -; Genomic_DNA.
DR   PIR; G83139; G83139.
DR   RefSeq; NP_252733.1; NC_002516.2.
DR   RefSeq; WP_003102816.1; NZ_QZGE01000013.1.
DR   AlphaFoldDB; Q9KGU7; -.
DR   SMR; Q9KGU7; -.
DR   STRING; 287.DR97_3823; -.
DR   PaxDb; Q9KGU7; -.
DR   PRIDE; Q9KGU7; -.
DR   EnsemblBacteria; AAG07431; AAG07431; PA4044.
DR   GeneID; 879037; -.
DR   KEGG; pae:PA4044; -.
DR   PATRIC; fig|208964.12.peg.4235; -.
DR   PseudoCAP; PA4044; -.
DR   HOGENOM; CLU_009227_1_4_6; -.
DR   InParanoid; Q9KGU7; -.
DR   OMA; QVGYHAQ; -.
DR   PhylomeDB; Q9KGU7; -.
DR   BioCyc; PAER208964:G1FZ6-4117-MON; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IBA:GO_Central.
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:0016744; F:transketolase or transaldolase activity; IBA:GO_Central.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central.
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   Gene3D; 3.40.50.920; -; 1.
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   PANTHER; PTHR43322; PTHR43322; 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; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   1: Evidence at protein level;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..627
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT                   /id="PRO_0000189142"
FT   BINDING         87
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         128..130
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         160..161
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         188
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         295
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         375
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   627 AA;  68050 MW;  EBEF04296FF6D57D CRC64;
     MPKTLHEIPR ERPATPLLDR ASSPAELRRL GEADLETLAD ELRQYLLYTV GQTGGHFGAG
     LGVVELTIAL HYVFDTPDDR LVWDVGHQAY PHKILTERRE LMGTLRQKNG LAAFPRRAES
     EYDTFGVGHS STSISAALGM AIAARLQGKE RKSVAVIGDG ALTAGMAFEA LNHASEVDAD
     MLVILNDNDM SISHNVGGLS NYLAKILSSR TYSSMREGSK KVLSRLPGAW EIARRTEEYA
     KGMLVPGTLF EELGWNYIGP IDGHDLPTLV ATLRNMRDMK GPQFLHVVTK KGKGFAPAEL
     DPIGYHAITK LEAPGSAPKK TGGPKYSSVF GQWLCDMAAQ DARLLGITPA MKEGSDLVAF
     SERYPERYFD VAIAEQHAVT LAAGMACEGM KPVVAIYSTF LQRAYDQLIH DVAVQHLDVL
     FAIDRAGLVG EDGPTHAGSF DISYLRCIPG MLVMTPSDED ELRKLLTTGY LFDGPAAVRY
     PRGSGPNHPI DPDLQPVEIG KGVVRRRGGR VALLVFGVQL AEAMKVAESL DATVVDMRFV
     KPLDEALVRE LAGSHELLVT IEENAVMGGA GSAVGEFLAS EGLEVPLLQL GLPDYYVEHA
     KPSEMLAECG LDAAGIEKAV RQRLDRQ
 
 
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