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Protein

1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic

Gene

DXR

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).By similarity

Catalytic activityi

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 divalent cation per subunit. Mg2+ or Mn2+.By similarity

Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

This protein is involved in step 1 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic (DXR)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ISPF)
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei136NADPBy similarity1
Binding sitei205SubstrateBy similarity1
Binding sitei206NADPBy similarity1
Metal bindingi231Divalent metal cationBy similarity1
Binding sitei232SubstrateBy similarity1
Metal bindingi233Divalent metal cationBy similarity1
Binding sitei293SubstrateBy similarity1
Metal bindingi315Divalent metal cationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi84 – 89NADPBy similarity6
Nucleotide bindingi113 – 117NADPBy similarity5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processIsoprene biosynthesis
LigandMagnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.1.1.267 4889
UniPathwayiUPA00056; UER00092

Names & Taxonomyi

Protein namesi
Recommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic (EC:1.1.1.267)
Short name:
1-deoxyxylulose-5-phosphate reductoisomerase
Short name:
DOXP reductoisomerase
Short name:
DXP reductoisomerase
Gene namesi
Name:DXR
ORF Names:PF14_0641
OrganismiPlasmodium falciparum (isolate 3D7)
Taxonomic identifieri36329 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
Proteomesi
  • UP000001450 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1467300

Subcellular locationi

GO - Cellular componenti

  • apicoplast Source: GeneDB

Keywords - Cellular componenti

Apicoplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 72ApicoplastBy similarityAdd BLAST72
ChainiPRO_000041560973 – 4881-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplasticAdd BLAST416

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1488
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi78 – 84Combined sources7
Helixi88 – 103Combined sources16
Beta strandi107 – 116Combined sources10
Helixi118 – 128Combined sources11
Beta strandi131 – 136Combined sources6
Helixi138 – 140Combined sources3
Helixi141 – 148Combined sources8
Beta strandi151 – 153Combined sources3
Beta strandi157 – 160Combined sources4
Helixi161 – 170Combined sources10
Beta strandi176 – 179Combined sources4
Helixi184 – 195Combined sources12
Beta strandi199 – 202Combined sources4
Helixi205 – 221Combined sources17
Beta strandi226 – 229Combined sources4
Helixi232 – 239Combined sources8
Helixi243 – 246Combined sources4
Beta strandi251 – 253Combined sources3
Helixi256 – 259Combined sources4
Beta strandi262 – 269Combined sources8
Turni273 – 276Combined sources4
Helixi279 – 284Combined sources6
Helixi287 – 291Combined sources5
Helixi300 – 308Combined sources9
Helixi310 – 323Combined sources14
Helixi327 – 329Combined sources3
Beta strandi330 – 334Combined sources5
Beta strandi340 – 346Combined sources7
Beta strandi351 – 355Combined sources5
Helixi361 – 369Combined sources9
Helixi383 – 386Combined sources4
Beta strandi388 – 390Combined sources3
Turni396 – 398Combined sources3
Helixi400 – 411Combined sources12
Helixi415 – 431Combined sources17
Helixi437 – 450Combined sources14
Helixi460 – 485Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4Y67X-ray1.60A/B75-488[»]
4Y6PX-ray1.90A/B75-488[»]
4Y6RX-ray1.90A/B75-488[»]
4Y6SX-ray2.10A/B75-488[»]
5JAZX-ray1.40A/B75-488[»]
5JBIX-ray1.70A/B75-488[»]
5JC1X-ray1.65A/B75-488[»]
5JMPX-ray1.70A/B75-488[»]
5JMWX-ray1.55A/B75-488[»]
5JNLX-ray1.60A/B75-488[»]
5JO0X-ray1.80A/B75-488[»]
ProteinModelPortaliQ8IKG4
SMRiQ8IKG4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 270Binding to substrate phosphate groupBy similarity2
Regioni311 – 315Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the DXR family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000007220
InParanoidiQ8IKG4
KOiK00099
OMAiDSEHFGL
PhylomeDBiQ8IKG4

Family and domain databases

HAMAPiMF_00183 DXP_reductoisom, 1 hit
InterProiView protein in InterPro
IPR003821 DXP_reductoisomerase
IPR013644 DXP_reductoisomerase_C
IPR013512 DXP_reductoisomerase_N
IPR026877 DXPR_C
IPR036169 DXPR_C_sf
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR30525 PTHR30525, 1 hit
PfamiView protein in Pfam
PF08436 DXP_redisom_C, 1 hit
PF02670 DXP_reductoisom, 1 hit
PF13288 DXPR_C, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69055 SSF69055, 1 hit
TIGRFAMsiTIGR00243 Dxr, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8IKG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKYIYIYFF FITITINDLV INNTSKCVSI ERRKNNAYIN YGIGYNGPDN
60 70 80 90 100
KITKSRRCKR IKLCKKDLID IGAIKKPINV AIFGSTGSIG TNALNIIREC
110 120 130 140 150
NKIENVFNVK ALYVNKSVNE LYEQAREFLP EYLCIHDKSV YEELKELVKN
160 170 180 190 200
IKDYKPIILC GDEGMKEICS SNSIDKIVIG IDSFQGLYST MYAIMNNKIV
210 220 230 240 250
ALANKESIVS AGFFLKKLLN IHKNAKIIPV DSEHSAIFQC LDNNKVLKTK
260 270 280 290 300
CLQDNFSKIN NINKIFLCSS GGPFQNLTMD ELKNVTSENA LKHPKWKMGK
310 320 330 340 350
KITIDSATMM NKGLEVIETH FLFDVDYNDI EVIVHKECII HSCVEFIDKS
360 370 380 390 400
VISQMYYPDM QIPILYSLTW PDRIKTNLKP LDLAQVSTLT FHKPSLEHFP
410 420 430 440 450
CIKLAYQAGI KGNFYPTVLN ASNEIANNLF LNNKIKYFDI SSIISQVLES
460 470 480
FNSQKVSENS EDLMKQILQI HSWAKDKATD IYNKHNSS
Length:488
Mass (Da):55,757
Last modified:March 1, 2003 - v1
Checksum:i4E280C81CDFAD3EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014187 Genomic DNA Translation: AAN37254.1
RefSeqiXP_001348815.1, XM_001348779.1

Genome annotation databases

GeneDBiPF3D7_1467300.1:pep
GeneIDi812223
KEGGipfa:PF14_0641

Similar proteinsi

Entry informationi

Entry nameiDXR_PLAF7
AccessioniPrimary (citable) accession number: Q8IKG4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: March 1, 2003
Last modified: October 25, 2017
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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