GenomeNet

Database: UniProt
Entry: DXS_XANCP
LinkDB: DXS_XANCP
Original site: DXS_XANCP 
ID   DXS_XANCP               Reviewed;         638 AA.
AC   Q8P815;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2002, sequence version 1.
DT   28-FEB-2018, entry version 99.
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=XCC2434;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 /
OS   NCPPB 528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM41711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE008922; AAM41711.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_637787.2; NC_003902.1.
DR   RefSeq; WP_011037575.1; NC_003902.1.
DR   ProteinModelPortal; Q8P815; -.
DR   SMR; Q8P815; -.
DR   STRING; 190485.XCC2434; -.
DR   EnsemblBacteria; AAM41711; AAM41711; XCC2434.
DR   GeneID; 1000936; -.
DR   KEGG; xcc:XCC2434; -.
DR   PATRIC; fig|190485.4.peg.2597; -.
DR   eggNOG; ENOG4105C2V; Bacteria.
DR   eggNOG; COG1154; LUCA.
DR   HOGENOM; HOG000012986; -.
DR   KO; K01662; -.
DR   OMA; AINHAGH; -.
DR   BioCyc; XCAM190485:G1FZM-2432-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000001010; Chromosome.
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;
KW   Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN         1    638       1-deoxy-D-xylulose-5-phosphate synthase.
FT                                /FTId=PRO_0000189176.
FT   REGION      120    122       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      152    153       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       151    151       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       182    182       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      79     79       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     182    182       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     291    291       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     373    373       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   638 AA;  68395 MW;  AD532238C52FF739 CRC64;
     MIDSTRYPRL SRIQTPDDLR TFEEADLTAV ADELRAYLIE SVGKSGGHFA AGLGVIELTV
     ALHYLYQTPV DQLVWDVGHQ TYPHKILTGR RDQIHTVKQK DGVAPFPKRE ESVYDTFGVG
     HSSTSISAAL GMAIAAQRNG DDRKVVAVIG DGAMTAGMVY EALNHAGGMD PEPNLLVILN
     DNRMSISEAV GGLTKMLGRA SGSRTLNAIR EGGKKILGDK KNNPTARFVR RWEEHWKGMF
     VPSTLFEEMG FHYTGPIDGH DLPSLVGALK TLKTLKGPQL LHVITTKGKG YELAEGDQIG
     YHAVGPFDPS KGLVAKAGAK KPTYTDVFSD WVCDMAAADP KMLVITPAMR EGSGLVRFSK
     EYPQRYFDVA IAEQHAVTLA AGMATQGAKP VVAIYSTFLQ RGYDQLVHDV AVQKLDVLFA
     IDRGGVVGPD GATHAGNLDL SFLRCVPHMV VMAPADEAEC RQMLTTGLRY EGPAAVRYPR
     GTGPGTALDA ALTTLPIGKA QLRHSGARIA LLGFGATVDA AEAVGRELGL TVVNMRFVKP
     LDKAMLLELA KCHEAFVSIE DNVVAGGAGS GVSELLNAEG VLMPMLHLGL PDSFQHHASR
     EDLLAEAGID QAGIRAAVLK RWPQLMAKGQ QALNAAAG
//
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