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Database: UniProt
Entry: A0A0D5NQ17_9BACL
LinkDB: A0A0D5NQ17_9BACL
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ID   A0A0D5NQ17_9BACL        Unreviewed;       631 AA.
AC   A0A0D5NQ17;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 21.
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=VN24_25210 {ECO:0000313|EMBL:AJY77250.1};
OS   Paenibacillus beijingensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY77250.1, ECO:0000313|Proteomes:UP000032633};
RN   [1] {ECO:0000313|Proteomes:UP000032633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA   Kwak Y., Shin J.-H.;
RT   "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL   Submitted (MAR-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; CP011058; AJY77250.1; -; Genomic_DNA.
DR   RefSeq; WP_045672675.1; NZ_CP011058.1.
DR   EnsemblBacteria; AJY77250; AJY77250; VN24_25210.
DR   KEGG; pbj:VN24_25210; -.
DR   PATRIC; fig|1126833.4.peg.5542; -.
DR   KO; K01662; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000032633; 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   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; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000032633};
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:SAAS00767590};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00767585};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032633};
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:SAAS00635456};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00315,
KW   ECO:0000256|SAAS:SAAS00635485, ECO:0000313|EMBL:AJY77250.1}.
FT   DOMAIN      314    479       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
FT   REGION      113    115       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   REGION      145    146       Thiamine pyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   METAL       144    144       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   METAL       173    173       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00315}.
FT   BINDING      72     72       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     173    173       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     284    284       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
FT   BINDING     365    365       Thiamine pyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   631 AA;  69345 MW;  EF18E15E55579D8C CRC64;
     MLLDNVNGPQ DLKAFTVPEL EQLAGEIREF LIRNLSVTGG HLAPNLGVVE LTLALHYLFN
     SPQDKFIFDV GHQSYVHKIL TGRMDRFSTL RKYKGLCGFV KRAESEHDVW EAGHSSTSLS
     AAMGMALARD LKGETNKVVA VIGDGALTGG MALEALNHIG HEKKNLIVIL NDNEMSIAPN
     VGALHSYLGK IRTDRHYQKA KEEVQSTLNR IPAIGGKLAK TIERFKDSLK YLLVSGILFE
     QFGFHYFGPV DGHDLNQLLE VLQQVESVQG PVLIHVVTVK GKGYLPAEAD SHKWHGITPY
     KIESGQVLKA VGPPMYTEVF GDALIELAEL DDRIIAVTPA MPGGSGLLKF AERFPGRMID
     VGIAEQHAAT MSAALALEGM KPVFAVYSTF LQRAYDQVVH DICRHQANVI FAIDRAGFVG
     PDGETHQGVY DIAFLRHIPN MVLMMPKDEN ELRNMLKTAV DYNEGPIAVR YPRINGLGVD
     IDPVMTPIPI GTWETVREGD SAVVLAIGPM LQTAEEAAEL LRREGIKLRI VNARFIKPLD
     EAMLLRLAEE GLNIFVMEEG SEMGGLGSAV LEFYSLHSIT GLKVKIIGVP DLFIEHGTIK
     EQRQETGLTA EKLAAEVIGA LPKRKRATNQ H
//
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