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O96693 (DXR_PLAFX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplast

Short name=1-deoxyxylulose-5-phosphate reductoisomerase
Short name=DOXP reductoisomerase
Short name=DXP reductoisomerase
EC=1.1.1.267
Gene names
Name:DXR
OrganismPlasmodium falciparum (isolate HB3)
Taxonomic identifier137071 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 divalent cation per subunit. Magnesium or manganese. Ref.2

Enzyme regulation

Inhibited by fosmidomycin and its derivative FT900098. Ref.1

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP-Rule MF_00183

Subunit structure

Homodimer. Ref.2

Subcellular location

Plastidapicoplast Ref.1.

Sequence similarities

Belongs to the DXR family.

Ontologies

Keywords
   Biological processIsoprene biosynthesis
   Cellular componentApicoplast
Plastid
   DomainTransit peptide
   LigandMagnesium
Manganese
Metal-binding
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentapicoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-deoxy-D-xylulose-5-phosphate reductoisomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NADPH binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7272Apicoplast Probable
Chain73 – 4884161-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplast HAMAP-Rule MF_00183
PRO_0000415608

Regions

Nucleotide binding84 – 896NADP HAMAP-Rule MF_00183
Nucleotide binding113 – 1175NADP HAMAP-Rule MF_00183
Region269 – 2702Binding to substrate phosphate group HAMAP-Rule MF_00183
Region311 – 3155Substrate binding HAMAP-Rule MF_00183

Sites

Metal binding2311Divalent metal cation
Metal binding2331Divalent metal cation
Metal binding3151Divalent metal cation
Binding site1361NADP
Binding site2051Substrate
Binding site2061NADP
Binding site2321Substrate
Binding site2931Substrate

Secondary structure

......................................................................... 488
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O96693 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4E280C81CDFAD3EF

FASTA48855,757
        10         20         30         40         50         60 
MKKYIYIYFF FITITINDLV INNTSKCVSI ERRKNNAYIN YGIGYNGPDN KITKSRRCKR 

        70         80         90        100        110        120 
IKLCKKDLID IGAIKKPINV AIFGSTGSIG TNALNIIREC NKIENVFNVK ALYVNKSVNE 

       130        140        150        160        170        180 
LYEQAREFLP EYLCIHDKSV YEELKELVKN IKDYKPIILC GDEGMKEICS SNSIDKIVIG 

       190        200        210        220        230        240 
IDSFQGLYST MYAIMNNKIV ALANKESIVS AGFFLKKLLN IHKNAKIIPV DSEHSAIFQC 

       250        260        270        280        290        300 
LDNNKVLKTK CLQDNFSKIN NINKIFLCSS GGPFQNLTMD ELKNVTSENA LKHPKWKMGK 

       310        320        330        340        350        360 
KITIDSATMM NKGLEVIETH FLFDVDYNDI EVIVHKECII HSCVEFIDKS VISQMYYPDM 

       370        380        390        400        410        420 
QIPILYSLTW PDRIKTNLKP LDLAQVSTLT FHKPSLEHFP CIKLAYQAGI KGNFYPTVLN 

       430        440        450        460        470        480 
ASNEIANNLF LNNKIKYFDI SSIISQVLES FNSQKVSENS EDLMKQILQI HSWAKDKATD 


IYNKHNSS 

« Hide

References

[1]"Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs."
Jomaa H., Wiesner J., Sanderbrand S., Altincicek B., Weidemeyer C., Hintz M., Turbachova I., Eberl M., Zeidler J., Lichtenthaler H.K., Soldati D., Beck E.
Science 285:1573-1576(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION.
Strain: Isolate HB3.
[2]"Molecular basis of fosmidomycin's action on the human malaria parasite Plasmodium falciparum."
Umeda T., Tanaka N., Kusakabe Y., Nakanishi M., Kitade Y., Nakamura K.T.
Sci. Rep. 1:E9-E9(2011)
Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEXES WITH NADPH; FOSMIDOMYCIN DERIVATIVE FR900098; MAGNESIUM AND MANGANESE, COFACTOR, SUBUNIT.
Strain: Isolate FCR-3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF111813 Genomic DNA. Translation: AAD03739.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AU8X-ray1.86A/B1-488[»]
3AU9X-ray1.90A/B1-488[»]
3AUAX-ray2.15A/B1-488[»]
4GAEX-ray2.30A/B75-488[»]
4KP7X-ray2.00A/B74-488[»]
ProteinModelPortalO96693.
SMRO96693. Positions 77-486.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.267. 1455.
UniPathwayUPA00056; UER00092.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00183. DXP_reductoisom.
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR026877. DXPR_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR30525. PTHR30525. 1 hit.
PfamPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
PF13288. DXPR_C. 1 hit.
[Graphical view]
SUPFAMSSF69055. SSF69055. 1 hit.
TIGRFAMsTIGR00243. Dxr. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO96693.

Entry information

Entry nameDXR_PLAFX
AccessionPrimary (citable) accession number: O96693
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways