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Database: UniProt
Entry: M5EH90_9RHIZ
LinkDB: M5EH90_9RHIZ
Original site: M5EH90_9RHIZ 
ID   M5EH90_9RHIZ            Unreviewed;       637 AA.
AC   M5EH90;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-SEP-2017, entry version 36.
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   ECO:0000313|EMBL:CCV03640.1};
GN   ORFNames=MESS2_110060 {ECO:0000313|EMBL:CCV03640.1};
OS   Mesorhizobium metallidurans STM 2683.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=1297569 {ECO:0000313|EMBL:CCV03640.1, ECO:0000313|Proteomes:UP000012062};
RN   [1] {ECO:0000313|EMBL:CCV03640.1, ECO:0000313|Proteomes:UP000012062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM 2683 {ECO:0000313|EMBL:CCV03640.1,
RC   ECO:0000313|Proteomes:UP000012062};
RA   Genoscope - CEA;
RL   Submitted (FEB-2013) 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: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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCV03640.1}.
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DR   EMBL; CAUM01000013; CCV03640.1; -; Genomic_DNA.
DR   RefSeq; WP_008872627.1; NZ_CAUM01000013.1.
DR   EnsemblBacteria; CCV03640; CCV03640; MESS2_110060.
DR   OrthoDB; POG091H015K; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000012062; Unassembled WGS sequence.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
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:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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   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 {ECO:0000313|Proteomes:UP000012062};
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:UP000012062};
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:CCV03640.1}.
FT   DOMAIN       35     54       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION      120    122       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      152    153       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       151    151       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       180    180       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      79     79       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     180    180       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     289    289       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     371    371       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   637 AA;  68018 MW;  76A811B0736038C6 CRC64;
     MNAKPDTPLL DKVRIPADLR TLAESELPQL ASELRAELID AVSHTGGHLG AGLGVVELTV
     ALHYVFNTPD DRLIWDVGHQ AYPHKILTGR RDRIRTLRQE GGLSGFTRRT ESEYDPFGAA
     HSSTSISAGL GMAMARDLCG GRNNVIAVIG DGAMSAGMAY EAMNNAGALD ARLIVILNDN
     DMSIAPPTGA MSAYLARLAS GKTYLGLRDF GKKLTSYLGE RADRAIKRAV EHARGYVTGG
     TLFEELGFYH IGPIDGHNLE HLIPVLKNVR DNADGPVLIH VVTQKGKGYG PAEAAPDKYH
     GVNKFDVITG AQAKAPANAP SYTKVFAESL IQEAREDDRI VAVTAAMPNG TGLDLFGEVF
     PTRTFDVGIA EQHAVTFAAG LATEGYRPFA AIYSTFLQRA YDQVVHDVAI QSLPVRFPID
     RAGFVGADGA THCGAFDTTF LATLPGFVVM AAADEAELRH MVRTAASYDD GPIAFRYPRG
     NGIGVDMPER GSVLEIGKGR IVREGTKVAL LSFGTRLQDC LAAADELGAA GLSTTVADAR
     FAKPLDEDMI RRLVRSHEVL VTVEEGAVGG FASHVLQFLA HEGLLESGLK VRPLVLPDVF
     TDHAKPEKMY ADAGLDSTGI VRTVFVALGH AASAQRA
//
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