GenomeNet

Database: UniProt
Entry: A0A0D9Y265_9ORYZ
LinkDB: A0A0D9Y265_9ORYZ
Original site: A0A0D9Y265_9ORYZ 
ID   A0A0D9Y265_9ORYZ        Unreviewed;       473 AA.
AC   A0A0D9Y265;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate reductoisomerase {ECO:0000256|ARBA:ARBA00012366};
DE            EC=1.1.1.267 {ECO:0000256|ARBA:ARBA00012366};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G00520.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM01G00520.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM01G00520.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-
CC         xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267;
CC         Evidence={ECO:0000256|ARBA:ARBA00034272};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC         Evidence={ECO:0000256|ARBA:ARBA00034272};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 1/6. {ECO:0000256|ARBA:ARBA00005094}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000256|ARBA:ARBA00006825}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0D9Y265; -.
DR   STRING; 40148.A0A0D9Y265; -.
DR   EnsemblPlants; OGLUM01G00520.1; OGLUM01G00520.1; OGLUM01G00520.
DR   Gramene; OGLUM01G00520.1; OGLUM01G00520.1; OGLUM01G00520.
DR   eggNOG; ENOG502QPJ7; Eukaryota.
DR   HOGENOM; CLU_035714_4_0_1; -.
DR   UniPathway; UPA00056; UER00092.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070402; F:NADPH binding; IEA:InterPro.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1740.10; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00183; DXP_reductoisom; 1.
DR   InterPro; IPR003821; DXP_reductoisomerase.
DR   InterPro; IPR013644; DXP_reductoisomerase_C.
DR   InterPro; IPR013512; DXP_reductoisomerase_N.
DR   InterPro; IPR026877; DXPR_C.
DR   InterPro; IPR036169; DXPR_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00243; Dxr; 1.
DR   PANTHER; PTHR30525; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE; 1.
DR   PANTHER; PTHR30525:SF0; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF08436; DXP_redisom_C; 1.
DR   Pfam; PF02670; DXP_reductoisom; 1.
DR   Pfam; PF13288; DXPR_C; 1.
DR   PIRSF; PIRSF006205; Dxp_reductismrs; 1.
DR   SUPFAM; SSF69055; 1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT   DOMAIN          79..207
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02670"
FT   DOMAIN          221..304
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08436"
FT   DOMAIN          336..458
FT                   /note="DXP reductoisomerase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13288"
SQ   SEQUENCE   473 AA;  51528 MW;  2D6AC64562E1278A CRC64;
     MALKVVSFPG DLAAVSFLDS NRGGAFNQLK VDLPFQRRDR RAVSLRRTCC SMQQAPPPAW
     PGRAVVEPGR RSWDGPKPIS IVGSTGSIGT QTLDIVAENP DKFRVVALAA GSNVTLLADQ
     VKTFKPKLVA VRNESLVDEL KEALADCDWK PEIIPGEQGV IEVARHPDAV TVVTGIVGCA
     GLKPTVAAIE AGKDIALANK ETLIAGGPFV LPLAQKHKVK ILPADSEHSA IFQCIQGLPE
     GALRRIILTA SGGAFRDWPV DKLKEVKVAD ALKHPNWNMG KKITVDSATL FNKGLEVIEA
     HYLFGAEYDD IEIVIHPQSI IHSMIETQDS SVLAQLGWPD MRIPILYTMS WPDRIYCSEV
     TWPRLDLCKL GSLTFKAPDN VKYPSMDLAY AAGRAGGTMT GVLSAANEKA VELFIDEKIG
     YLDIFKVVEL TCDAHRNELV TRPSLEEIIH YDLWAREYAA SLQPSTGLSP VPV
//
DBGET integrated database retrieval system