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P50648

- RIR1_PLAF4

UniProt

P50648 - RIR1_PLAF4

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RNR1

Organism
Plasmodium falciparum (isolate Dd2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

    Enzyme regulationi

    Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the large subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521Allosteric activatorBy similarity
    Binding sitei87 – 871Allosteric activatorBy similarity
    Binding sitei200 – 2001SubstrateBy similarity
    Sitei216 – 2161Important for hydrogen atom transferBy similarity
    Sitei224 – 2241Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
    Sitei254 – 2541Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei425 – 4251Proton acceptorBy similarity
    Active sitei427 – 4271Cysteine radical intermediateBy similarity
    Active sitei429 – 4291Proton acceptorBy similarity
    Sitei442 – 4421Important for hydrogen atom transferBy similarity
    Sitei737 – 7371Important for electron transferBy similarity
    Sitei738 – 7381Important for electron transferBy similarity
    Sitei801 – 8011Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei804 – 8041Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

    GO - Biological processi

    1. deoxyribonucleotide biosynthetic process Source: UniProtKB
    2. DNA replication Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase R1 subunit
    Gene namesi
    Name:RNR1
    OrganismiPlasmodium falciparum (isolate Dd2)
    Taxonomic identifieri57267 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 806806Ribonucleoside-diphosphate reductase large subunitPRO_0000187198Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi216 ↔ 442Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.

    Structurei

    3D structure databases

    ProteinModelPortaliP50648.
    SMRiP50648. Positions 15-762.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9191ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 177Allosteric activator bindingBy similarity
    Regioni215 – 2162Substrate bindingBy similarity
    Regioni283 – 2864Allosteric effector binding, determines substrate specificityBy similarity
    Regioni425 – 4295Substrate bindingBy similarity
    Regioni603 – 6075Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.

    Family and domain databases

    InterProiIPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50648-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYVLNRKGEE EDISFDQILK RIQRLSYGLH ELVDPARVTQ GVINGMYSGI    50
    KTCELDELAA QTCAYMATTH PDFSILAARI TTDNLHKNTS DDVAEVAEAL 100
    YTYKDVRGRP ASLISKEVYD FILLHKDRLN KEIDYTRDFN YDYFGFKTLE 150
    RSYLLRINNK IIERPQHLLM RVSIGIHIDD IDKALETYHL MSQKYFTHAT 200
    PTLFNSGTPR PQMSSCFLLS MKADSIEGIF ETLKQCALIS KTAGGIGVAV 250
    QDIRGQNSYI RGTNGISNGL VPMLRVFNDT ARYVDQGGGK RKGSFAVYIE 300
    PWHSDIFEFL DLRKNHGKEE LRARDLFYAV WVPDLFMKRV KENKNWTLMC 350
    PNECPGLSET WGEEFEKLYT KYEEENMGKK TVLAQDLWFA ILQSQIETGV 400
    PYMLYKDSCN AKSNQKNLGT IKCSNLCCEI IEYTSPDEVA VCNLASIALC 450
    KFVDLEKKEF NFKKLYEITK IITRNLDKII ERNYYPVKEA KTSNTRHRPI 500
    GIGVQGLADT FMLLRYPYES DAAKELNKRI FETMYYAALE MSVELASIHG 550
    PYESYQGSPA SQGILQFDMW NAKVDNKYWD WDELKAKIRK HGLRNSLLLA 600
    PMPTASTSQI LGNNESFEPY TSNIYYRRVL SGEFFVVNPH LLKDLFDRGL 650
    WDEDMKQQLI AHNGSIQYIS EIPDDLKELY KTVWEIKQKN IIDMAADRGI 700
    FIDQSQSLNI YIQKPTFAKL SSMHFYGWEK GLKTGAYYLR TQAATDAIKF 750
    TVDTHVAKNA VKLKNADGVQ ITREVSRETI STESTVTQNV CPLRRNNDEQ 800
    CLMCSG 806
    Length:806
    Mass (Da):92,513
    Last modified:October 1, 1996 - v1
    Checksum:iA23B414A687B275F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01323 mRNA. Translation: AAA50171.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01323 mRNA. Translation: AAA50171.1 .

    3D structure databases

    ProteinModelPortali P50648.
    SMRi P50648. Positions 15-762.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0209.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of subunit genes of ribonucleotide reductase, a cell-cycle-regulated enzyme, from Plasmodium falciparum."
      Chakrabarti D., Schuster S.M., Chakrabarti R.
      Proc. Natl. Acad. Sci. U.S.A. 90:12020-12024(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiRIR1_PLAF4
    AccessioniPrimary (citable) accession number: P50648
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3