ID   DXR_ARATH               Reviewed;         477 AA.
AC   Q9XFS9; Q9M6U2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   04-NOV-2026, entry version 177.
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 {ECO:0000250|UniProtKB:P45568};
DE   AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase;
DE   AltName: Full=Protein PIGMENT-DEFECTIVE EMBRYO 129;
DE   Flags: Precursor;
GN   Name=DXR; Synonyms=ISPC, PDE129; OrderedLocusNames=At5g62790;
GN   ORFNames=MQB2.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=12177470; DOI=10.1104/pp.003798;
RA   Carretero-Paulet L., Ahumada I., Cunillera N., Rodriguez-Concepcion M.,
RA   Ferrer A., Boronat A., Campos N.;
RT   "Expression and molecular analysis of the Arabidopsis DXR gene encoding 1-
RT   deoxy-D-xylulose 5-phosphate reductoisomerase, the first committed enzyme
RT   of the 2-C-methyl-D-erythritol 4-phosphate pathway.";
RL   Plant Physiol. 129:1581-1591(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 72-477.
RC   STRAIN=cv. Columbia;
RX   PubMed=10428488; DOI=10.1016/s0014-5793(99)00849-2;
RA   Schwender J., Mueller C., Zeidler J., Lichtenthaler H.K.;
RT   "Cloning and heterologous expression of a cDNA encoding 1-deoxy-D-xylulose-
RT   5-phosphate reductoisomerase of Arabidopsis thaliana.";
RL   FEBS Lett. 455:140-144(1999).
RN   [8]
RP   INDUCTION.
RX   PubMed=15863698; DOI=10.1104/pp.104.058735;
RA   Hsieh M.H., Goodman H.M.;
RT   "The Arabidopsis IspH homolog is involved in the plastid nonmevalonate
RT   pathway of isoprenoid biosynthesis.";
RL   Plant Physiol. 138:641-653(2005).
RN   [9]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=16941216; DOI=10.1007/s11103-006-9051-9;
RA   Carretero-Paulet L., Cairo A., Botella-Pavia P., Besumbes O., Campos N.,
RA   Boronat A., Rodriguez-Concepcion M.;
RT   "Enhanced flux through the methylerythritol 4-phosphate pathway in
RT   Arabidopsis plants overexpressing deoxyxylulose 5-phosphate
RT   reductoisomerase.";
RL   Plant Mol. Biol. 62:683-695(2006).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18236010; DOI=10.1007/s11103-008-9297-5;
RA   Hsieh M.H., Chang C.Y., Hsu S.J., Chen J.J.;
RT   "Chloroplast localization of methylerythritol 4-phosphate pathway enzymes
RT   and regulation of mitochondrial genes in ispD and ispE albino mutants in
RT   Arabidopsis.";
RL   Plant Mol. Biol. 66:663-673(2008).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20404857; DOI=10.1038/cr.2010.54;
RA   Xing S., Miao J., Li S., Qin G., Tang S., Li H., Gu H., Qu L.J.;
RT   "Disruption of the 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR)
RT   gene results in albino, dwarf and defects in trichome initiation and
RT   stomata closure in Arabidopsis.";
RL   Cell Res. 20:688-700(2010).
CC   -!- FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid
CC       biosynthesis that catalyzes the NADPH-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.
CC       {ECO:0000269|PubMed:12177470, ECO:0000269|PubMed:16941216,
CC       ECO:0000269|PubMed:20404857}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-
CC         xylulose 5-phosphate + NADPH + H(+); 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:0000250|UniProtKB:P45568};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719;
CC         Evidence={ECO:0000250|UniProtKB:P45568};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P45568};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P45568};
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:0000305|PubMed:16941216}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000305|PubMed:12177470, ECO:0000305|PubMed:18236010}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9XFS9-1; Sequence=Displayed;
CC   -!- INDUCTION: Circadian-regulated with a peak in the late period of the
CC       light phase. {ECO:0000269|PubMed:12177470,
CC       ECO:0000269|PubMed:15863698}.
CC   -!- DISRUPTION PHENOTYPE: Albino and dwarf phenotype.
CC       {ECO:0000269|PubMed:20404857}.
CC   -!- MISCELLANEOUS: Plants over-expressing DXR show increased levels of
CC       plastid isoprenoids derived from the methylerythritol 4-phosphate (MEP)
CC       pathway, such as chlorophylls, carotenoids, and taxadiene.
CC       {ECO:0000305|PubMed:16941216}.
CC   -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}.
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DR   EMBL; AF148852; AAF73140.1; -; mRNA.
DR   EMBL; AB009053; BAB10848.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97657.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7057533.1; -; Genomic_DNA.
DR   EMBL; AY045634; AAK73992.1; -; mRNA.
DR   EMBL; AY050802; AAK92737.1; -; mRNA.
DR   EMBL; AY054682; AAK96873.1; -; mRNA.
DR   EMBL; AY081453; AAM10015.1; -; mRNA.
DR   EMBL; AY091405; AAM14344.1; -; mRNA.
DR   EMBL; AY098952; AAM19962.1; -; mRNA.
DR   EMBL; AY084775; AAM61343.1; -; mRNA.
DR   EMBL; AJ242588; CAB43344.1; -; mRNA.
DR   PIR; T52570; T52570.
DR   RefSeq; NP_201085.1; NM_125674.3. [Q9XFS9-1]
DR   AlphaFoldDB; Q9XFS9; -.
DR   SMR; Q9XFS9; -.
DR   BioGRID; 21643; 2.
DR   FunCoup; Q9XFS9; 956.
DR   STRING; 3702.Q9XFS9; -.
DR   BindingDB; Q9XFS9; -.
DR   ChEMBL; CHEMBL2285354; -.
DR   iPTMnet; Q9XFS9; -.
DR   PaxDb; 3702-Q9XFS9; -.
DR   ProteomicsDB; 222040; -. [Q9XFS9-1]
DR   GeneID; 836400; -.
DR   KEGG; ath:AT5G62790; -.
DR   Araport; AT5G62790; -.
DR   TAIR; AT5G62790; DXR.
DR   eggNOG; ENOG502QPJ7; Eukaryota.
DR   HOGENOM; CLU_035714_4_0_1; -.
DR   InParanoid; Q9XFS9; -.
DR   OMA; AAACCDF; -.
DR   PhylomeDB; Q9XFS9; -.
DR   BioCyc; ARA:AT5G62790-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G62790-MONOMER; -.
DR   BRENDA; 1.1.1.267; 399.
DR   UniPathway; UPA00056; UER00092.
DR   PRO; PR:Q9XFS9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Proteomes; UP001984100; Chromosome 5.
DR   ExpressionAtlas; Q9XFS9; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0070402; F:NADPH binding; IEA:InterPro.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway; IDA:TAIR.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; TAS:TAIR.
DR   FunFam; 1.10.1740.10:FF:000006; 1-deoxy-D-xylulose 5-phosphate reductoisomerase, chloroplastic; 1.
DR   FunFam; 3.40.50.720:FF:000183; 1-deoxy-D-xylulose 5-phosphate reductoisomerase, chloroplastic; 1.
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   NCBIfam; NF009114; PRK12464.1; 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   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   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Isoprene biosynthesis; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..477
FT                   /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase,
FT                   chloroplastic"
FT                   /id="PRO_0000007395"
FT   REGION          56..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         90
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         91
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         92
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         115
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         117
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         203
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         204
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         205
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         229
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         230
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         231
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         231
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         255
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         278
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         284
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         291
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         296
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         297
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         300
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
FT   BINDING         300
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P45568"
SQ   SEQUENCE   477 AA;  51964 MW;  C06A455AB73ACA7C CRC64;
     MMTLNSLSPA ESKAISFLDT SRFNPIPKLS GGFSLRRRNQ GRGFGKGVKC SVKVQQQQQP
     PPAWPGRAVP EAPRQSWDGP KPISIVGSTG SIGTQTLDIV AENPDKFRVV ALAAGSNVTL
     LADQVRRFKP ALVAVRNESL INELKEALAD LDYKLEIIPG EQGVIEVARH PEAVTVVTGI
     VGCAGLKPTV AAIEAGKDIA LANKETLIAG GPFVLPLANK HNVKILPADS EHSAIFQCIQ
     GLPEGALRKI ILTASGGAFR DWPVEKLKEV KVADALKHPN WNMGKKITVD SATLFNKGLE
     VIEAHYLFGA EYDDIEIVIH PQSIIHSMIE TQDSSVLAQL GWPDMRLPIL YTMSWPDRVP
     CSEVTWPRLD LCKLGSLTFK KPDNVKYPSM DLAYAAGRAG GTMTGVLSAA NEKAVEMFID
     EKISYLDIFK VVELTCDKHR NELVTSPSLE EIVHYDLWAR EYAANVQLSS GARPVHA
//