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Database: UniProt
Entry: W4VCW4_9BACI
LinkDB: W4VCW4_9BACI
Original site: W4VCW4_9BACI 
ID   W4VCW4_9BACI            Unreviewed;       309 AA.
AC   W4VCW4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=1-deoxy-D-xylulose 5-phosphate synthase {ECO:0000313|EMBL:GAE91255.1};
GN   ORFNames=JCM21714_200 {ECO:0000313|EMBL:GAE91255.1};
OS   Gracilibacillus boraciitolerans JCM 21714.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=1298598 {ECO:0000313|EMBL:GAE91255.1, ECO:0000313|Proteomes:UP000019102};
RN   [1] {ECO:0000313|EMBL:GAE91255.1, ECO:0000313|Proteomes:UP000019102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21714 {ECO:0000313|EMBL:GAE91255.1,
RC   ECO:0000313|Proteomes:UP000019102};
RA   Ahmed I., Oshima K., Suda W., Kitamura K., Iida T., Ohmori Y., Fujiwara T.,
RA   Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of the Boron-Tolerant and Moderately Halotolerant
RT   Bacterium Gracilibacillus boraciitolerans JCM 21714T.";
RL   Genome Announc. 2:e00097-14(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE91255.1}.
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DR   EMBL; BAVS01000001; GAE91255.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4VCW4; -.
DR   STRING; 1298598.JCM21714_200; -.
DR   eggNOG; COG1154; Bacteria.
DR   Proteomes; UP000019102; Unassembled WGS sequence.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd02007; TPP_DXS; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR049557; Transketolase_CS.
DR   PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43322:SF5; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019102};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   309 AA;  34381 MW;  5FF0601F4707C0D3 CRC64;
     MDLTKMKNPK FLKELNTEEL EILAAEIRQF LINKLSVTGG HLGANLGVVE LTLALHKQFN
     SPKDKLIFDV GHQSYIHKML TGRTDQFDTL RQFKGLCGFP KMNESEHDVW ETGHSSTSLS
     AAMGMAIARD MKKEKNFVVP IIGDGALTGG MALEALNHIG HEKKNLTVIL NDNEMSIAGN
     VGALHNALGR MRSAGKYNRV KDELEVLLKR IPAVGGKIAQ TAERVKDSMK YFMVPGMLFE
     EFGFTYFGPV DGHDFRDLEK HIAYAKKTEG PVLIHVITQK GKGYKPAEMD EKDKWHGVGP
     YKIDSGGRK
//
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