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O15909

- RIR1_TRYBB

UniProt

O15909 - RIR1_TRYBB

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RNR1

Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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 sitei10 – 101Allosteric activatorBy similarity
    Binding sitei58 – 581Allosteric activatorBy similarity
    Binding sitei93 – 931Allosteric activatorBy similarity
    Binding sitei212 – 2121SubstrateBy similarity
    Sitei228 – 2281Important for hydrogen atom transferBy similarity
    Sitei236 – 2361Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei257 – 2571Substrate; via amide nitrogenBy similarity
    Sitei266 – 2661Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei437 – 4371Proton acceptorBy similarity
    Active sitei439 – 4391Cysteine radical intermediateBy similarity
    Active sitei441 – 4411Proton acceptorBy similarity
    Sitei454 – 4541Important for hydrogen atom transferBy similarity
    Sitei759 – 7591Important for electron transferBy similarity
    Sitei760 – 7601Important for electron transferBy similarity
    Sitei833 – 8331Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei836 – 8361Interacts 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
    OrganismiTrypanosoma brucei brucei
    Taxonomic identifieri5702 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 838838Ribonucleoside-diphosphate reductase large subunitPRO_0000187199Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi228 ↔ 454Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit.

    Structurei

    3D structure databases

    ProteinModelPortaliO15909.
    SMRiO15909. Positions 23-777.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 9792ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni16 – 227Allosteric activator bindingBy similarity
    Regioni227 – 2282Substrate bindingBy similarity
    Regioni295 – 2984Allosteric effector binding, determines substrate specificityBy similarity
    Regioni437 – 4415Substrate bindingBy similarity
    Regioni625 – 6295Substrate 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.

    O15909-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLETVKLVTK RDGSVEPYDE KVVRSRIVNL MSGIDSYYVD VDDLVRVVGE    50
    GVREGMSTSM LDELLAETAA YCVTKHPDYG LLAGRLAVTA LHKTTTESVL 100
    DSFRVLHEHV SQATKRHAPL ISEELWDIAN KHSAALQQII NYERDFDFEY 150
    FGYKTLERSY LLRVHKGRGV MEVVERPQQM FLRVALGIHG EDLERVKETY 200
    DYMSQGFFTH ATPTLFNAGT PFPQMSSCFL VAMREDSIDG IYDTLKQCAI 250
    ISKSAGGIGI HMHNIRAAGS YIAGTNGTSN GLVPMLRVWN NTARYVDQGG 300
    GKRKGAFAIY LEPWHADIFG FLLLKKNTGK EDQRARDLFY GLWIPDLFME 350
    RVESHGTWTL MDPNTAPFLS DCYGQEFTDL YERYEREGRG VRTIQAQELW 400
    FLILESQVET GVPFMLYKDA CNFKSNQKNL GTIKCSNLCT EIVEYTSRDE 450
    VAVCNLASIA LPRFVKDGAF DYVALKEVTK VVTRNLNRVI DRNHYPVCEA 500
    RYSNLRHRPV GIGVQGLADA FALLSLPFAH PEAKKLNRQI FETIYIAAVE 550
    ASTELAEKDG PYETFKGSPA SEGKLQFDLW DEERRIRGMN EDSVHSHCGL 600
    WDWDSLKERV VKVGMRNSLL IAPMPTASTS QILGNNECIE PFTSNIYVRR 650
    VLSGEFPVVN KHLVKELIRL RLWNDDMRRK IIALNGSVSG IKEIPERIRE 700
    LYKVVWEIRQ KDLIDMAADR GRYIDQSQSL NLFLATPTSS QLTSMHFYSW 750
    KKGLKTGMYY LRSQPAADAI KFTLDPKAMK ELPKPDKQSK EEVHGSVGRG 800
    KRKRVGEKPT ANHSNAGAPN LNGPPDTDGD GGCLNCGS 838
    Length:838
    Mass (Da):94,619
    Last modified:January 1, 1998 - v1
    Checksum:i19A9B95525BAF69A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80910 mRNA. Translation: AAB70704.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U80910 mRNA. Translation: AAB70704.1 .

    3D structure databases

    ProteinModelPortali O15909.
    SMRi O15909. Positions 23-777.
    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 and characterization of the R1 and R2 subunits of ribonucleotide reductase from Trypanosoma brucei."
      Hofer A., Schmidt P.P., Graslund A., Thelander L.
      Proc. Natl. Acad. Sci. U.S.A. 94:6959-6964(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 427.

    Entry informationi

    Entry nameiRIR1_TRYBB
    AccessioniPrimary (citable) accession number: O15909
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 73 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