ID I1N1T9_SOYBN Unreviewed; 714 AA.
AC I1N1T9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 64.
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 Name=100814637 {ECO:0000313|EnsemblPlants:KRG99484};
GN ORFNames=GLYMA_18G148700 {ECO:0000313|EMBL:KRG99484.1};
OS Glycine max (Soybean) (Glycine hispida).
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=3847 {ECO:0000313|EMBL:KRG99484.1};
RN [1] {ECO:0000313|EMBL:KRG99484.1, ECO:0000313|EnsemblPlants:KRG99484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG99484};
RC TISSUE=Callus {ECO:0000313|EMBL:KRG99484.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRG99484}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG99484};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRG99484.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRG99484.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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; CM000851; KRG99484.1; -; Genomic_DNA.
DR RefSeq; XP_003552082.1; XM_003552034.3.
DR AlphaFoldDB; I1N1T9; -.
DR SMR; I1N1T9; -.
DR STRING; 3847.I1N1T9; -.
DR PaxDb; 3847-GLYMA18G28830-1; -.
DR EnsemblPlants; KRG99484; KRG99484; GLYMA_18G148700.
DR GeneID; 100814637; -.
DR Gramene; KRG99484; KRG99484; GLYMA_18G148700.
DR KEGG; gmx:100814637; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_1_4_1; -.
DR InParanoid; I1N1T9; -.
DR OMA; QIGKQTH; -.
DR OrthoDB; 3626892at2759; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000008827; Chromosome 18.
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:0016744; F:transketolase or transaldolase activity; IBA:GO_Central.
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 Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 394..559
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 714 AA; 77092 MW; E362753DB4DC21C3 CRC64;
MAFCGGTFVK LNYSVSPCHK YKAPSPYHSY RNKFCVRVSA SGSADEERTI IKKEKDGWKI
NYAGEKPATL LLDTINYPIH MKNLSTQDLE QLAAELRADI VHTVSNTGGH LSSSLGVVEL
AVALHHVFNT PEDKIIWDVG HQAYPHKILT GRRSRMHTIR KTSGLAGFPK RDESIHDAFG
VGHSSTSISA GLGMAVARDL LGKNNSIISV IGDGALTAGQ AYEAMNNAGF LDSNMIVVLN
DNKQVSLPTA TLDGPASPVG ALSSALSKIQ ASAEFRKLRE AAKSITKQIG KQTHQVAAKV
DEYARGIISG SACTFFEELG LYYIGPVDGH KIEDLVTIFE KVKAMPAPGP VLIHCVTEKG
KGYPPAEKAS DKMHGVVKFD PKTGEQFKAK SSTLSYTQYF AESLIKEAEN DKKIVAIHAA
MGGGTGLNYF HKRFPERCFD VGIAEQHAVT FAAGLAAEGL KPFCAIYSSF LQRGYDQVVH
DVDLQKLPVR FALDRAGLVG ADGPTHCGAF DITYMACLPN MVVMAPSDEA ELMHMVATAA
AIDDRPSCFR FPRGNGIGAT LPLNNKGTPL EIGKGRILVE GSRIAILGYG SVVQQCRQAS
EMLKELGVDV TVADARFCKP LDTGLIRLLA KEHEILITVE EGSIGGFGSH VSQFLSLSGI
LDGPLKWRAM MLPDRYIEHG SPQAQVEDAG LSSKHIAATV LSLMERPKQA LLFK
//
