(data stored in ACNUC7421 zone)

SWISSPROT: DXS_PARXL

ID   DXS_PARXL               Reviewed;         635 AA.
AC   Q13RX1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 75.
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=Bxeno_B0200; ORFNames=Bxe_B2827;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C
CC       atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield
CC       1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {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-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_00315};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose
CC       5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; CP000271; ABE33168.1; -; Genomic_DNA.
DR   RefSeq; WP_011490544.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13RX1; -.
DR   SMR; Q13RX1; -.
DR   STRING; 266265.Bxe_B2827; -.
DR   EnsemblBacteria; ABE33168; ABE33168; Bxe_B2827.
DR   GeneID; 4006574; -.
DR   KEGG; bxb:DR64_5156; -.
DR   KEGG; bxe:Bxe_B2827; -.
DR   PATRIC; fig|266265.5.peg.4866; -.
DR   eggNOG; ENOG4105C2V; Bacteria.
DR   eggNOG; COG1154; LUCA.
DR   HOGENOM; HOG000012986; -.
DR   KO; K01662; -.
DR   OMA; AINHAGH; -.
DR   OrthoDB; POG091H015K; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
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   InterPro; IPR005474; Transketolase_N.
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; 3.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13RX1.
DR   SWISS-2DPAGE; Q13RX1.
KW   Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN         1    635       1-deoxy-D-xylulose-5-phosphate synthase.
FT                                /FTId=PRO_0000256393.
FT   REGION      115    117       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      147    148       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       146    146       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       176    176       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      74     74       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     176    176       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     283    283       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     365    365       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   635 AA;  68228 MW;  DF9A2188FA89D031 CRC64;
     MYDLLKTIDD PAALRRLDRR QLQPLADELR AFVLDSVSQT GGHLSSNLGT VELTIALHYV
     FDTPHDRIVW DVGHQTYPHK ILTGRRDQMH TLRQLGGISG FPKRDESEYD TFGTAHSSTS
     ISAALGMAVA SKLKGDNRMG IAVIGDGAMT AGMAFEAMNN AGVEDDVPLL VILNDNDMSI
     SPPVGALNRH LARLMSGRFY AAARAGVERV LRVAPPMLDL ARKLEEHAKG MIVPATLFEE
     FGFNYIGPID GHDLDSLIPT LQNIKELRGP QFLHVVTKKG QGYKLAEADP VLYHGPGKFN
     PAEGIKPAAT PSKKTYTQVF GEWLCDAAEL DARVIGITPA MREGSGMVEF EKRFPDRYFD
     VGIAEQHAVT FAGGLAAEGM KPVVAIYSTF LQRAYDQLIH DVALQNLPVV FAIDRAGLVG
     ADGATHAGAY DLAFLRCIPN MTVMAASDEN ECRQMLYTAL QQPNPTAVRY PRGAGTGVAT
     IKQMTALPLG KGEIRRETSQ PAGKRIAILA FGTMVAPSLA AAEQLDATVA NMRFVKPLDA
     DLVRQLAETH DAIVTVEEGC VMGGAGSACV EALLASGVTR PVLQLGLPDR FIDHGDPAKL
     LAACGLDAVG ITKSIRERFL LSGAVGGQSS VKRVA
//

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