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Entry: A0A127B1G8_9BACT
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ID   A0A127B1G8_9BACT        Unreviewed;       638 AA.
AC   A0A127B1G8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 13.
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   ORFNames=TH61_09085 {ECO:0000313|EMBL:AMM51293.1};
OS   Rufibacter sp. DG15C.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=1379909 {ECO:0000313|EMBL:AMM51293.1, ECO:0000313|Proteomes:UP000070672};
RN   [1] {ECO:0000313|EMBL:AMM51293.1, ECO:0000313|Proteomes:UP000070672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG15C {ECO:0000313|EMBL:AMM51293.1,
RC   ECO:0000313|Proteomes:UP000070672};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Rufibacter sp. DG15C whole genome sequencing.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; CP010776; AMM51293.1; -; Genomic_DNA.
DR   RefSeq; WP_066508450.1; NZ_CP010776.1.
DR   EnsemblBacteria; AMM51293; AMM51293; TH61_09085.
DR   KEGG; rud:TH61_09085; -.
DR   PATRIC; fig|1379909.4.peg.1962; -.
DR   KO; K01662; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000070672; Chromosome.
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; 2.
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:UP000070672};
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:UP000070672};
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:AMM51293.1}.
FT   DOMAIN       34     53       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION      119    121       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      78     78       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     180    180       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     292    292       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     377    377       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   638 AA;  70594 MW;  79851F6C936FB60F CRC64;
     MIIEPGELLS KIDSPADLRK LSEDQLLQVC QELRQFIIDN VSIYGGHFGA SLGVVEMTVA
     LHYVFNTPYD QLVWDVGHQA YGHKILTGRR DNFHTNRKLN GISGFPKRKE SEYDAFGVGH
     SSTSISAALG MAVASQIKKE FDRHHIAVIG DGSMTAGMAF EALNHGGATD ADLLVILNDN
     CMSIDPNVGA LKEYLTDITT SRTYNKVRDE LWNILGKISK FGPNAQQIAS KVESGIKATL
     LKQSNLFESL KFRYFGPIDG HDVNHLASVL QDLKKIPGPK ILHCVTVKGK GFALAEKEQT
     KWHAPGLFDK VTGEIYKVHH TTPQPPKYQD VFGHTLLEMA EQNPKIMGVT PAMPSGSSMN
     IMMAAMPDRA IDVGIAEQHA VTFSAGLATQ GMVPFCNIYS SFMQRGYDQV VHDVCLQNLH
     VVFTLDRAGF AGADGQTHHG SYDIAFMRCL PNMVVSSPMN EQELRNLMFT ASQDGMGPFT
     IRYPRGEGVM PEWRTPLELI EVGKGRTVQE GEEVAVLTIG HIGNYVVDVC KNLKLDGLRP
     GHYDMRFCKP LDEKLLHHIF QKYDKVVTVE DGCLQGGFGS AILEFMADHG YNAQVKRLGI
     PDTIVEHGSQ LELHRLCGFD PEGIERAVRE LMEVTVRV
//
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