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Q5R919

- RIR1_PONAB

UniProt

Q5R919 - RIR1_PONAB

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

RRM1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

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

    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 M1 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 sitei5 – 51Allosteric activatorBy similarity
    Binding sitei53 – 531Allosteric activatorBy similarity
    Binding sitei88 – 881Allosteric activatorBy similarity
    Binding sitei202 – 2021SubstrateBy similarity
    Sitei218 – 2181Important for hydrogen atom transferBy similarity
    Sitei226 – 2261Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
    Sitei256 – 2561Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei427 – 4271Proton acceptorBy similarity
    Active sitei429 – 4291Cysteine radical intermediateBy similarity
    Active sitei431 – 4311Proton acceptorBy similarity
    Sitei444 – 4441Important for hydrogen atom transferBy similarity
    Sitei737 – 7371Important for electron transferBy similarity
    Sitei738 – 7381Important for electron transferBy similarity
    Sitei787 – 7871Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei790 – 7901Interacts 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):
    Ribonucleoside-diphosphate reductase subunit M1
    Ribonucleotide reductase large subunit
    Gene namesi
    Name:RRM1
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 792792Ribonucleoside-diphosphate reductase large subunitPRO_0000290352Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171N6-acetyllysineBy similarity
    Disulfide bondi218 ↔ 444Redox-activeBy similarity
    Modified residuei376 – 3761N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    PRIDEiQ5R919.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit. Interacts with RRM2B By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R919.
    SMRiQ5R919. Positions 15-759.
    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
    Regioni217 – 2182Substrate bindingBy similarity
    Regioni285 – 2884Allosteric effector binding, determines substrate specificityBy similarity
    Regioni427 – 4315Substrate bindingBy similarity
    Regioni603 – 6075Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG003447.
    InParanoidiQ5R919.
    KOiK10807.

    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.

    Q5R919-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG    50
    VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKEA KKVFSDVMED 100
    LYNYINPHNG KHSPMVAKST LDIVLANKDR LNSAIIYDRD FSYNYFGFKT 150
    LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSERWFTH 200
    ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV 250
    AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY 300
    LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL 350
    MCPNECPGLD EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET 400
    GTPYMLYKDS CNRKSNQQNL GTIKCSSLCT EIVEYTSKDE VAVCNLASLA 450
    LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI IDINYYPVPE ACLSNKRHRP 500
    IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL EASCDLAKEQ 550
    GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKLLKEKIAK YGIRNSLLIA 600
    PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL 650
    WHEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA 700
    FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF 750
    TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS LENRDECLMC GS 792
    Length:792
    Mass (Da):90,027
    Last modified:December 21, 2004 - v1
    Checksum:i93AC48CB6CEEC044
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859577 mRNA. Translation: CAH91741.1.
    RefSeqiNP_001126012.1. NM_001132540.2.
    UniGeneiPab.9179.

    Genome annotation databases

    GeneIDi100172956.
    KEGGipon:100172956.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859577 mRNA. Translation: CAH91741.1 .
    RefSeqi NP_001126012.1. NM_001132540.2.
    UniGenei Pab.9179.

    3D structure databases

    ProteinModelPortali Q5R919.
    SMRi Q5R919. Positions 15-759.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5R919.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100172956.
    KEGGi pon:100172956.

    Organism-specific databases

    CTDi 6240.

    Phylogenomic databases

    HOVERGENi HBG003447.
    InParanoidi Q5R919.
    KOi K10807.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Heart.

    Entry informationi

    Entry nameiRIR1_PONAB
    AccessioniPrimary (citable) accession number: Q5R919
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 12, 2007
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on M1, is formed only in the presence of the second subunit M2 By similarity.By similarity

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3