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Database: UniProt
Entry: B5YE06
LinkDB: B5YE06
Original site: B5YE06 
ID   DXS_DICT6               Reviewed;         618 AA.
AC   B5YE06;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   26-NOV-2014, entry version 48.
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=DICTH_0902;
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Dictyoglomus thermophilum strain ATCC
RT   35947 / DSM 3960 / H-6-12.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001146; ACI19059.1; -; Genomic_DNA.
DR   RefSeq; WP_012547691.1; NC_011297.1.
DR   RefSeq; YP_002250764.1; NC_011297.1.
DR   ProteinModelPortal; B5YE06; -.
DR   STRING; 309799.DICTH_0902; -.
DR   EnsemblBacteria; ACI19059; ACI19059; DICTH_0902.
DR   GeneID; 6945851; -.
DR   KEGG; dth:DICTH_0902; -.
DR   PATRIC; 21806440; VBIDicThe33784_0885.
DR   eggNOG; COG1154; -.
DR   HOGENOM; HOG000012987; -.
DR   KO; K01662; -.
DR   OMA; ELRNIMY; -.
DR   OrthoDB; EOG6BKJ6P; -.
DR   BioCyc; DTHE309799:GHF9-895-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 3.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005476; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
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.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN         1    618       1-deoxy-D-xylulose-5-phosphate synthase.
FT                                /FTId=PRO_1000115737.
FT   REGION      113    115       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      145    146       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       144    144       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       173    173       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      72     72       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     173    173       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     284    284       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     359    359       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   618 AA;  68238 MW;  7FFEABD5B900B482 CRC64;
     MLLQKINSPK DLKRLSIDEL KTLSAEIREI IINTVENNGG HLASNLGTVE LTLALHYVFD
     TPEDKIIWDV GHQAYTHKLV TGRAKDFHTL RQFGGISGYI APWESEYDHF AVGHAGTSLS
     AALGFAKARD LKGEKYKVIA VIGDGALTSG MALEALNQIG YLNTDLIVVL NDNEHSISPN
     VGAIALYLAK LRKHPLYRFF KQTTQNLLKN SSIGKGLLAF DLKLERSLKS LLLENPMFEY
     WGFKYFGPFD GHDIPVLISV FKGIKDNLSC PVLIHITTKK GIGHKDAEAT PSKFHSIGAK
     IEREKKVPTY TEVFGKALVE LGEKYPEIVA ITAAMPEGTG LSYFAQRFPE RFFDVGIAEE
     HAVTFAAGLA KNGLKPVVAI YSTFLQRAFD QIIHDVCLQK LPIVFVLDRA GIVSDDGPTH
     QGIFDLSYLR LIPNMVISAP KDESELRDLL YTAINYPGPF AIRYPKSKGV GIGLKDHFER
     IEIGKSEILK YGKNVLILAI GSMVYPALEA ESILKTEGIS PTIVNVRFLK PLDVLTLEEL
     ISSHDVIITV EENVITGGLF GAISELVNIL KLNKKVLPIS LPDKFIEQGN AQLLRDIYGL
     SGHKIAEKII SVLEDVKV
//
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