Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O96693

- DXR_PLAFX

UniProt

O96693 - DXR_PLAFX

Protein

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

Gene

DXR

Organism
Plasmodium falciparum (isolate HB3)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 divalent cation per subunit. Magnesium or manganese.1 Publication

    Enzyme regulationi

    Inhibited by fosmidomycin and its derivative FT900098.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei136 – 1361NADP
    Binding sitei205 – 2051Substrate
    Binding sitei206 – 2061NADP
    Metal bindingi231 – 2311Divalent metal cation
    Binding sitei232 – 2321Substrate
    Metal bindingi233 – 2331Divalent metal cation
    Binding sitei293 – 2931Substrate
    Metal bindingi315 – 3151Divalent metal cation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi84 – 896NADP
    Nucleotide bindingi113 – 1175NADP

    GO - Molecular functioni

    1. 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. NADPH binding Source: InterPro

    GO - Biological processi

    1. isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway Source: UniProtKB-UniPathway

    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. 1455.
    UniPathwayiUPA00056; UER00092.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplast (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 lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

    Subcellular locationi

    Plastidapicoplast 1 Publication

    GO - Cellular componenti

    1. apicoplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apicoplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7272ApicoplastCuratedAdd
    BLAST
    Chaini73 – 4884161-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastPRO_0000415608Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    488
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi78 – 847
    Helixi88 – 10316
    Beta strandi107 – 11610
    Helixi118 – 12811
    Beta strandi131 – 1366
    Helixi138 – 1403
    Helixi142 – 1454
    Helixi147 – 1504
    Beta strandi157 – 1604
    Helixi161 – 17010
    Beta strandi176 – 1794
    Helixi183 – 19513
    Beta strandi199 – 2024
    Helixi206 – 22116
    Beta strandi226 – 2294
    Helixi232 – 2409
    Helixi243 – 2464
    Beta strandi251 – 2533
    Helixi256 – 2594
    Beta strandi262 – 2698
    Turni273 – 2764
    Helixi279 – 2824
    Turni287 – 2893
    Helixi301 – 3077
    Helixi310 – 32314
    Helixi327 – 3293
    Beta strandi330 – 3345
    Beta strandi340 – 3467
    Beta strandi351 – 3555
    Helixi361 – 3699
    Helixi383 – 3864
    Beta strandi388 – 3903
    Turni396 – 3983
    Helixi400 – 41112
    Helixi415 – 43117
    Helixi437 – 45014
    Helixi460 – 48324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO96693.
    SMRiO96693. Positions 77-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO96693.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 2702Binding to substrate phosphate group
    Regioni311 – 3155Substrate binding

    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.
    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]
    SUPFAMiSSF69055. 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

    MKKYIYIYFF FITITINDLV INNTSKCVSI ERRKNNAYIN YGIGYNGPDN    50
    KITKSRRCKR IKLCKKDLID IGAIKKPINV AIFGSTGSIG TNALNIIREC 100
    NKIENVFNVK ALYVNKSVNE LYEQAREFLP EYLCIHDKSV YEELKELVKN 150
    IKDYKPIILC GDEGMKEICS SNSIDKIVIG IDSFQGLYST MYAIMNNKIV 200
    ALANKESIVS AGFFLKKLLN IHKNAKIIPV DSEHSAIFQC LDNNKVLKTK 250
    CLQDNFSKIN NINKIFLCSS GGPFQNLTMD ELKNVTSENA LKHPKWKMGK 300
    KITIDSATMM NKGLEVIETH FLFDVDYNDI EVIVHKECII HSCVEFIDKS 350
    VISQMYYPDM QIPILYSLTW PDRIKTNLKP LDLAQVSTLT FHKPSLEHFP 400
    CIKLAYQAGI KGNFYPTVLN ASNEIANNLF LNNKIKYFDI SSIISQVLES 450
    FNSQKVSENS EDLMKQILQI HSWAKDKATD IYNKHNSS 488
    Length:488
    Mass (Da):55,757
    Last modified:May 1, 1999 - v1
    Checksum:i4E280C81CDFAD3EF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF111813 Genomic DNA. Translation: AAD03739.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF111813 Genomic DNA. Translation: AAD03739.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AU8 X-ray 1.86 A/B 1-488 [» ]
    3AU9 X-ray 1.90 A/B 1-488 [» ]
    3AUA X-ray 2.15 A/B 1-488 [» ]
    4GAE X-ray 2.30 A/B 75-488 [» ]
    4KP7 X-ray 2.00 A/B 74-488 [» ]
    ProteinModelPortali O96693.
    SMRi O96693. Positions 77-486.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00056 ; UER00092 .
    BioCyci MetaCyc:MONOMER-18397.
    BRENDAi 1.1.1.267. 1455.

    Miscellaneous databases

    EvolutionaryTracei O96693.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_00183. DXP_reductoisom.
    InterProi IPR003821. DXP_reductoisomerase.
    IPR013644. DXP_reductoisomerase_C.
    IPR013512. DXP_reductoisomerase_N.
    IPR026877. DXPR_C.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR30525. PTHR30525. 1 hit.
    Pfami PF08436. DXP_redisom_C. 1 hit.
    PF02670. DXP_reductoisom. 1 hit.
    PF13288. DXPR_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69055. SSF69055. 1 hit.
    TIGRFAMsi TIGR00243. Dxr. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 66 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

    External Data

    Dasty 3