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Database: UniProt
Entry: A0A098UKE5_9BURK
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ID   A0A098UKE5_9BURK        Unreviewed;       592 AA.
AC   A0A098UKE5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   05-DEC-2018, entry version 28.
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=IA69_01510 {ECO:0000313|EMBL:KGF83493.1};
OS   Massilia sp. JS1662.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Massilia.
OX   NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF83493.1, ECO:0000313|Proteomes:UP000029701};
RN   [1] {ECO:0000313|EMBL:KGF83493.1, ECO:0000313|Proteomes:UP000029701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS1662 {ECO:0000313|EMBL:KGF83493.1,
RC   ECO:0000313|Proteomes:UP000029701};
RA   Fida T.T., Spain J.C.;
RT   "Identification of Arachidin-3 degrading bacteria in the peanut
RT   rhizosphere.";
RL   Submitted (JUL-2014) 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:SAAS01090567}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-
CC         D-xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57792, ChEBI:CHEBI:59776; EC=2.2.1.7;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00315,
CC         ECO:0000256|SAAS:SAAS01090541};
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:SAAS01090565}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00315,
CC       ECO:0000256|SAAS:SAAS01090540}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00315, ECO:0000256|SAAS:SAAS01090559}.
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:KGF83493.1}.
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DR   EMBL; JPQD01000001; KGF83493.1; -; Genomic_DNA.
DR   RefSeq; WP_036228055.1; NZ_JPQD01000001.1.
DR   EnsemblBacteria; KGF83493; KGF83493; IA69_01510.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000029701; 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; 2.
DR   Pfam; PF13292; DXP_synthase_N; 2.
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:UP000029701};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS01090549};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086467};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086515};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029701};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS01090534};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086495};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00086511, ECO:0000313|EMBL:KGF83493.1}.
FT   DOMAIN       29     48       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
FT   REGION      114    116       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      146    147       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       145    145       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       175    175       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      73     73       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     175    175       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     250    250       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     331    331       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   592 AA;  62032 MW;  B18428B54AF11CC7 CRC64;
     MDLLEAINDP AALRALPRAR LDTLARQLRR FLLDTVARTG GHLASNLGTV ELTIALHYVF
     ATPRDRIVWD VGHQSYGHKV LTGRRAQMHT LRQAGGLSGF PRRCESVHDC FGTAHSSTAL
     SAALGMALAA KLRGDDRHAV AVCGDGALSA GMAFEALNNA GVDPSLRLLV VVNHNGMSIS
     SAVGALDRHL SDLATGRVRP GASLFEAVGF AYAGPVDGHD LDALIPALEA ARRRTGPQVL
     HVVTRKGKGY APAEAAPTLY HGTGRFDPGK GLPDGARGRP AYTDVFGDWL CDMAAHDPRL
     VGITPAMREG SGLVRFAQRY PDRYVDVGIA EQHALTFAGG LAADGMKPVV AIYSTFLQRA
     YDQLIHDVAL QHLDVTFAID RAGLVGADGA THAGNYDIAY LRCVPGMVLM AASDEAECRR
     MLTTAYRHPG PAAVRYPRGP GPGVVPAAGL DVIPLGRGEV RRRGSGIAIL AFGPMLAPSL
     EAGAELGATV ANMRFVKPLD VDLVLALARD HAQLVTVEEG AVMGGAGAAV AEALAAAGIQ
     RPLLMLGLPD LFIEHGDPAA LLGAAGLDAA GIAGAIRQRY RADAPLLVAN SH
//
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