(data stored in SCRATCH zone)

SWISSPROT: C3MHG3_SINFN

ID   C3MHG3_SINFN            Unreviewed;       645 AA.
AC   C3MHG3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 72.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000256|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000256|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000256|HAMAP-Rule:MF_00315};
GN   OrderedLocusNames=NGR_c04950 {ECO:0000313|EMBL:ACP24291.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24291.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24291.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS00767580}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000256|HAMAP-
CC       Rule:MF_00315, ECO:0000256|SAAS:SAAS00767589}.
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:0000256|HAMAP-Rule:MF_00315, ECO:0000256|SAAS:SAAS00767582}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00315,
CC       ECO:0000256|SAAS:SAAS00767578}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|SAAS:SAAS00767545}.
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DR   EMBL; CP001389; ACP24291.1; -; Genomic_DNA.
DR   RefSeq; WP_012707076.1; NC_012587.1.
DR   RefSeq; YP_002825044.1; NC_012587.1.
DR   STRING; 394.NGR_c04950; -.
DR   EnsemblBacteria; ACP24291; ACP24291; NGR_c04950.
DR   GeneID; 7791721; -.
DR   KEGG; rhi:NGR_c04950; -.
DR   PATRIC; fig|394.7.peg.3304; -.
DR   eggNOG; ENOG4105C2V; Bacteria.
DR   eggNOG; COG1154; LUCA.
DR   HOGENOM; HOG000012988; -.
DR   KO; K01662; -.
DR   OMA; AINHAGH; -.
DR   OrthoDB; POG091H015K; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000001054; Chromosome.
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   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; C3MHG3.
DR   SWISS-2DPAGE; C3MHG3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767552};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767540};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00651241, ECO:0000313|EMBL:ACP24291.1}.
FT   DOMAIN       40     59       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION      125    127       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      157    158       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       156    156       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       185    185       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      84     84       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     185    185       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     294    294       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     376    376       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   645 AA;  68751 MW;  25FBB6ADFA72D239 CRC64;
     MTQLPTNPMP ATPLLDKVNV PDDLKKIDDR DLPQLASELR SEMIDAVSRT GGHLGAGLGV
     VELTIAIHKV FDTPHDRLIF DVGHQCYPHK ILTGRRDRIR TLRQEGGLSG FTRRAESEYD
     PFGAAHSSTS ISAGLGMAVA ADLDGKSRNV IAVIGDGALS AGMAYEALNN AGALDARLIV
     ILNDNDMSIA PPTGAMSAYL ARLASGRTYM GIREVGKKLT AYLGKTVDRA ITRAVEHARG
     YVTGGTLFEE MGFYHIGPID GHSFDHLLPV LRNVRDNRRG PVLIHVVTQK GKGYPPAEAA
     ADKYHGVNKF DVITGAQAKA KPNAPAYTSV FADALTQEAS LDDKIVAITA AMPHGTGLDR
     FAAVHPSRCF DVGIAEQHAV TFAAGLAAEG YKPFAALYST FLQRAYDQVV HDVAIQGLPV
     RFPIDRAGFV GADGPTHAGS FDTTYLASLP GFVVMAAADE AELKHMVRTA AAYDDGPISF
     RYPRGEGVGV ELPERGEILE IGKGRIIKQG TKVALLSFGT RLADCLLAAE DLDAAGLSTT
     VADARFAKPL DHELIRQLAR HHEVLITIEE GAIGGFASHV LHFLAEEGLL DGGLKVRPMV
     LPDIWMEQAK PESMYAAAGL DRVGIVSTVF KALGQKHSVG LGAAG
//

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