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P50647

- RIR1_PLAFG

UniProt

P50647 - RIR1_PLAFG

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RNR1

Organism
Plasmodium falciparum (isolate FCR-3 / Gambia)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (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 sitei53 – 531Allosteric activatorBy similarity
    Binding sitei88 – 881Allosteric activatorBy similarity
    Binding sitei201 – 2011SubstrateBy similarity
    Sitei217 – 2171Important for hydrogen atom transferBy similarity
    Sitei225 – 2251Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
    Sitei255 – 2551Allosteric 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
    Sitei736 – 7361Important for electron transferBy similarity
    Sitei737 – 7371Important for electron transferBy similarity
    Sitei799 – 7991Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei802 – 8021Interacts 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 FCR-3 / Gambia)
    Taxonomic identifieri5838 [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 – 804804Ribonucleoside-diphosphate reductase large subunitPRO_0000187197Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi217 ↔ 442Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.

    Structurei

    3D structure databases

    ProteinModelPortaliP50647.
    SMRiP50647. Positions 15-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 177Allosteric activator bindingBy similarity
    Regioni216 – 2172Substrate bindingBy similarity
    Regioni284 – 2874Allosteric effector binding, determines substrate specificityBy similarity
    Regioni425 – 4295Substrate bindingBy similarity
    Regioni602 – 6065Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    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.

    P50647-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYVLNRKGEE EDISFDQILK RIQRLSYGLH KLGEYPACVT QGVINGMYSS    50
    IKTCELDELA AQTCAYMATT HPDFSILAAR ITTDNLHKNT SDDVAEVAEA 100
    LYTYKDGRGR PASLISKEVY DFILLHKVRL NKEIDYTTHF NYDYFGFKTL 150
    ERSYLLRINN KIIERPQHLL MRVSIGIHID DIDKALETYH LMSQKYFTHA 200
    TPTLFNSGTP RPQMSSCFLL SMKADSIEGI FETLKQCALI SKTAGGIGVA 250
    VQDIRGQNSY IRGTNGISNG LVPMLRVFND TARYVDQGGG KRKGSYAVYI 300
    EPWHSDIFEF LDLRKNHGKE ELRARDLFYA VWVPDLFMKR VKENKNWTLM 350
    CPNECPGLSE TWGEEFEKLY TKYEEENMGK KTVLAQDLWF AILQSQIETG 400
    VPIYLYKDSC NAKPIKNLGT IKCSNLCCEI IEYTSPDEVA VCNLASIALC 450
    KFVDLEKKEF NFKKLYEITK IITRNLDKII ERNYYPVKEA KTSNTRHRPI 500
    GIGVQGLADT FMLLRYLYES DAAKELNKRI YETMYYAALE MSVDWLQSGP 550
    YESYQGSPGS QGILQFDMWN AKVDNKYWDW DELKLKIAKT GLRNLLLLAP 600
    MPTASTSQIL GNNESFEPYT SNIYYRRVLS GEFFVVNPHL LKDLFDRGLW 650
    DEDMKQQLIA HNGSIQYISE IPDDLKELYK TVWEIKQKNI IDMAADRGYF 700
    IDQSQSLNIY IQKPTFAKLS SMHFYGWEKG LKTGAYYLRT QAATDAIKFT 750
    VDTHVAKNAV KLKNADGVQI TREVSRETIQ LNQRYSKCVS FKSNNDEQCL 800
    MCSG 804
    Length:804
    Mass (Da):92,403
    Last modified:October 1, 1996 - v1
    Checksum:i8D3C70EA2ED0A6E9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF205580 Genomic DNA. Translation: AAA29755.1.
    PIRiB48687.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF205580 Genomic DNA. Translation: AAA29755.1 .
    PIRi B48687.

    3D structure databases

    ProteinModelPortali P50647.
    SMRi P50647. Positions 15-761.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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, sequence determination, and regulation of the ribonucleotide reductase subunits from Plasmodium falciparum: a target for antimalarial therapy."
      Rubin H., Salem J.S., Li L.S., Yang F.D., Mama S., Wang Z.M., Fisher A., Hamann C.S., Cooperman B.S.
      Proc. Natl. Acad. Sci. U.S.A. 90:9280-9284(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiRIR1_PLAFG
    AccessioniPrimary (citable) accession number: P50647
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 74 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