DXR_ARATH
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 03-AUG-2022, entry version 159.
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 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 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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION.
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 [9]
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 [10]
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 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.
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 + 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
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}.
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 EMBL; AF148852; AAF73140.1; -; mRNA.
DR EMBL; AB009053; BAB10848.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97657.1; -; 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 STRING; 3702.AT5G62790.2; -.
DR BindingDB; Q9XFS9; -.
DR ChEMBL; CHEMBL2285354; -.
DR iPTMnet; Q9XFS9; -.
DR PaxDb; Q9XFS9; -.
DR PRIDE; Q9XFS9; -.
DR ProteomicsDB; 222040; -. [Q9XFS9-1]
DR EnsemblPlants; AT5G62790.1; AT5G62790.1; AT5G62790. [Q9XFS9-1]
DR GeneID; 836400; -.
DR Gramene; AT5G62790.1; AT5G62790.1; AT5G62790. [Q9XFS9-1]
DR KEGG; ath:AT5G62790; -.
DR Araport; AT5G62790; -.
DR eggNOG; ENOG502QPJ7; Eukaryota.
DR HOGENOM; CLU_035714_4_0_1; -.
DR InParanoid; Q9XFS9; -.
DR OMA; FIDGSVM; -.
DR PhylomeDB; Q9XFS9; -.
DR BioCyc; ARA:AT5G62790-MON; -.
DR BioCyc; MetaCyc:AT5G62790-MON; -.
DR BRENDA; 1.1.1.267; 399.
DR UniPathway; UPA00056; UER00092.
DR PRO; PR:Q9XFS9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XFS9; baseline and differential.
DR Genevisible; Q9XFS9; AT.
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 SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69055; SSF69055; 1.
DR TIGRFAMs; TIGR00243; Dxr; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Isoprene biosynthesis; Metal-binding;
KW NADP; Oxidoreductase; Plastid; Reference proteome; 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 86..115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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
