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Protein

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

Gene

DXR

Organism
Plasmodium falciparum (isolate HB3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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).1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 1 divalent cation per subunit. Mg2+ or Mn2+.1 Publication

Enzyme regulationi

Inhibited by fosmidomycin and its derivative FT900098.1 Publication

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 sitei136NADP1
Binding sitei205Substrate1
Binding sitei206NADP1
Metal bindingi231Divalent metal cation1
Binding sitei232Substrate1
Metal bindingi233Divalent metal cation1
Binding sitei293Substrate1
Metal bindingi315Divalent metal cation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi84 – 89NADP6
Nucleotide bindingi113 – 117NADP5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Isoprene biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18397.
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
OrganismiPlasmodium falciparum (isolate HB3)
Taxonomic identifieri137071 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Apicoplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 72ApicoplastCuratedAdd BLAST72
ChainiPRO_000041560873 – 4881-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplasticAdd BLAST416

Interactioni

Subunit structurei

Homodimer.1 Publication

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
Helixi142 – 145Combined sources4
Helixi147 – 150Combined sources4
Beta strandi151 – 153Combined sources3
Beta strandi157 – 160Combined sources4
Helixi161 – 170Combined sources10
Beta strandi176 – 179Combined sources4
Helixi183 – 195Combined sources13
Beta strandi199 – 202Combined sources4
Helixi206 – 221Combined sources16
Beta strandi226 – 229Combined sources4
Helixi232 – 240Combined sources9
Helixi243 – 246Combined sources4
Beta strandi251 – 253Combined sources3
Helixi256 – 259Combined sources4
Beta strandi262 – 269Combined sources8
Turni273 – 276Combined sources4
Helixi279 – 282Combined sources4
Turni287 – 289Combined sources3
Helixi301 – 307Combined sources7
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 – 483Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AU8X-ray1.86A/B1-488[»]
3AU9X-ray1.90A/B1-488[»]
3AUAX-ray2.15A/B1-488[»]
3WQQX-ray2.25A/B1-488[»]
3WQRX-ray1.97A/B1-488[»]
3WQSX-ray2.35B1-488[»]
4GAEX-ray2.30A/B75-488[»]
4KP7X-ray2.00A/B74-488[»]
ProteinModelPortaliO96693.
SMRiO96693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO96693.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 270Binding to substrate phosphate group2
Regioni311 – 315Substrate binding5

Sequence similaritiesi

Belongs to the DXR family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom. 1 hit.
InterProiIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR30525. PTHR30525. 1 hit.
PfamiPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
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.

O96693-1 [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:May 1, 1999 - v1
Checksum:i4E280C81CDFAD3EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF111813 Genomic DNA. Translation: AAD03739.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF111813 Genomic DNA. Translation: AAD03739.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AU8X-ray1.86A/B1-488[»]
3AU9X-ray1.90A/B1-488[»]
3AUAX-ray2.15A/B1-488[»]
3WQQX-ray2.25A/B1-488[»]
3WQRX-ray1.97A/B1-488[»]
3WQSX-ray2.35B1-488[»]
4GAEX-ray2.30A/B75-488[»]
4KP7X-ray2.00A/B74-488[»]
ProteinModelPortaliO96693.
SMRiO96693.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00056; UER00092.
BioCyciMetaCyc:MONOMER-18397.
BRENDAi1.1.1.267. 4889.

Miscellaneous databases

EvolutionaryTraceiO96693.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00183. DXP_reductoisom. 1 hit.
InterProiIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR30525. PTHR30525. 1 hit.
PfamiPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69055. SSF69055. 1 hit.
TIGRFAMsiTIGR00243. Dxr. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDXR_PLAFX
AccessioniPrimary (citable) accession number: O96693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.