ID A0A0B2QWW2_GLYSO Unreviewed; 714 AA.
AC A0A0B2QWW2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|ARBA:ARBA00013150};
DE EC=2.2.1.7 {ECO:0000256|ARBA:ARBA00013150};
GN ORFNames=glysoja_036362 {ECO:0000313|EMBL:KHN24127.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN24127.1};
RN [1] {ECO:0000313|EMBL:KHN24127.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN24127.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000256|ARBA:ARBA00011081}.
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DR EMBL; KN655706; KHN24127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2QWW2; -.
DR OrthoDB; 3626892at2759; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000053555; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02007; TPP_DXS; 1.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR049557; Transketolase_CS.
DR NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF4; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE 2, CHLOROPLASTIC-RELATED; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KHN24127.1}.
FT DOMAIN 394..559
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 714 AA; 76827 MW; 27AC2ECE1DB6C4DE CRC64;
MTFCGGAFVK PNYSVSPCHK HKAPSPYQGG RNKFCVRVSA SGSADEERTI IRKEKDGWKI
NYSGEKPATP LLDTVNHPIH MKNLSTQDLE QLAAELRADI VHSVSDTGGH LSSSLGVVEL
SVALHHVFNT PEDKIIWDVG HQAYPHKILT GRRSRMHTIR KSSGLAGFPK RDESVHDAFG
VGHSSTSISA GLGMAVARDL LGKNNSIISV IGDGALTAGQ AYEAMNNAGF LDSNMIVVLN
DNKQVSLPTA TLDGPATPVG ALSSALSKIQ ASSEFRKLRE AAKTITKQIG GQTHQVAAKV
DEYARGMISA SGSTLFEELG LYYIGPVDGH NIEDLVTIFE KVKAMPAPGP VLIHVVTEKG
KGYPPAEKAA DRMHGVVKFD PKTGQQFKAK TSTLSYTQYF AESLIKEAEN DKKIVAIHAA
MGGGTGLNYF HKRFPKRCFD VGIAEQHAVT FAAGLAAEGL KPFCAIYSSF LQRGYDQVVH
DVDLQKLPVR FAMDRAGLVG ADGPTHCGAF DIAYMACLPN MVVMAPSDEA ELMHMVATAA
AIDDRPSCFR FPRGNGIGAT LPLNNKGTSL EIGKGRILVE GSRVAILGYG SVVQQCRQAS
EMLKELGIDV TVADARFCKP LDTGLIRLLA KEHEILITVE EGSIGGFGSH VSQFLSLSGI
LDGPLKWRAM MLPDRYIEHG SPQVQIEEAG LSSKQIAATV LSLMERPNEA LLFK
//
