DXR_ORYSJ
ID DXR_ORYSJ Reviewed; 473 AA.
AC Q8W250; A0A0N7KC68; Q0JRD4; Q9FTN0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase, chloroplastic;
DE Short=1-deoxyxylulose-5-phosphate reductoisomerase;
DE Short=DXP reductoisomerase;
DE EC=1.1.1.267;
DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase;
DE Flags: Precursor;
GN Name=DXR; OrderedLocusNames=Os01g0106900, LOC_Os01g01710;
GN ORFNames=OsJ_00058, P0005A05.24, P0482C06.2;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Carretero-Paulet L., Boronat A., Campos N.;
RT "1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), catalyzing the
RT first committed step of the mevalonate-independent pathway for IPP
RT biosynthesis.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid
CC biosynthesis that catalyzes the NADP-dependent rearrangement and
CC reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-
CC erythritol 4-phosphate (MEP). Required for chloroplast development (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 1/6.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC -!- INDUCTION: By the mycorrhizal fungus G.intraradices colonization in
CC roots.
CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}.
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DR EMBL; AF367205; AAL37560.1; -; mRNA.
DR EMBL; AP002845; BAB78606.1; -; Genomic_DNA.
DR EMBL; AP002863; BAB16915.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF03694.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS69977.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE53719.1; -; Genomic_DNA.
DR EMBL; AK099702; BAG94262.1; -; mRNA.
DR RefSeq; XP_015618768.1; XM_015763282.1.
DR AlphaFoldDB; Q8W250; -.
DR SMR; Q8W250; -.
DR STRING; 4530.OS01T0106900-01; -.
DR PaxDb; Q8W250; -.
DR PRIDE; Q8W250; -.
DR EnsemblPlants; Os01t0106900-01; Os01t0106900-01; Os01g0106900.
DR EnsemblPlants; Os01t0106900-02; Os01t0106900-02; Os01g0106900.
DR GeneID; 4326153; -.
DR Gramene; Os01t0106900-01; Os01t0106900-01; Os01g0106900.
DR Gramene; Os01t0106900-02; Os01t0106900-02; Os01g0106900.
DR KEGG; osa:4326153; -.
DR eggNOG; ENOG502QPJ7; Eukaryota.
DR HOGENOM; CLU_035714_4_0_1; -.
DR InParanoid; Q8W250; -.
DR OMA; PIDSEHF; -.
DR OrthoDB; 1128719at2759; -.
DR PlantReactome; R-OSA-1119464; Methylerythritol phosphate pathway.
DR UniPathway; UPA00056; UER00092.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q8W250; OS.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0051484; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process; IBA:GO_Central.
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 PANTHER; PTHR30525; PTHR30525; 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69055; SSF69055; 1.
DR TIGRFAMs; TIGR00243; Dxr; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Isoprene biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..473
FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase,
FT chloroplastic"
FT /id="PRO_0000247469"
FT BINDING 82..111
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 128
FT /note="L -> H (in Ref. 1; AAL37560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 51473 MW; 9933D9D8C3D1FC49 CRC64;
MALKVVSFPG DLAAVSFLDS NRGGAFNQLK VDLPFQTRDR 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
