ID A0A0E0L7M6_ORYPU Unreviewed; 723 AA.
AC A0A0E0L7M6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|ARBA:ARBA00013150};
DE EC=2.2.1.7 {ECO:0000256|ARBA:ARBA00013150};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC06G02590.3};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC06G02590.3}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC06G02590.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0L7M6; -.
DR EnsemblPlants; OPUNC06G02590.3; OPUNC06G02590.3; OPUNC06G02590.
DR Gramene; OPUNC06G02590.3; OPUNC06G02590.3; OPUNC06G02590.
DR HOGENOM; CLU_009227_1_4_1; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000026962; Chromosome 6.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
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 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; IPR033248; Transketolase_C.
DR NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF3; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 403..568
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 370..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 79343 MW; 9146E53885D57981 CRC64;
MGVTYLHSPP AVNLVFEESA LVHSTSCRLH SSQCLGCNTS KLKPCRTLVF NLPSRRFNRR
VAALPDVDDF FWEKDPTPIL DTIDAPIHLK NLSSKVELKQ LAGEVRSEIS FIMSRKCQPC
NTGHSVVDLA IAIHYVFNAP MDKILWDAGQ HTYAHKILTG RRSLFHTIKQ RKGLSGFTSR
FESEYDPFGA GHGCNSLSAG LGMAVARDLG GRKNRIVTVI SNWTTMAGQV YEAMGHAGFL
DSNMVVILND SRHTLLPKPD SQSKMSINAF SSALSKVQSS KGFRKFREAA KGLSKWFGKG
MHEFAAKIDE YARGMIGPHG ATLFEELGLY YIGPIDGNNI DDLICVLKEV ATLDSTGPVL
VHVITENEKD SGGDFNSEVT PNEEGPPESS QDILKFLENG LSRTYNDCFV ESLIAEAEND
KRIVVVHGGM GIDRSIQLFQ SRFPDRFFDL GIAEQHAVTF SAGLACGGLK PFCIIPSTFL
QRAYDQIVED VDMQKIPVRF AITSAGLVGS EGPTNSGPFD ITFMSCLPNM IVMSPSNEDE
LIDMVATAAM VEDRPICFRY PRGAIVGTSG TLAYGNPLEI GKGEILAEGK EIAFLGYGEV
VQRCLIARSL LFNFGIQATV ANARFCKPLD IDLIRMLCQQ HDFLITVEEG TVGGFGSHVS
QFISLDGLLD GKIKWRPIVL PDRYIEHASL TEQLDMAGLT AHHIAATALT LLGRHRDALL
LMK
//
