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P0A5W9

- RIR1_MYCBO

UniProt

P0A5W9 - RIR1_MYCBO

Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdE

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      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. 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 By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei172 – 1721SubstrateBy similarity
    Sitei189 – 1891Important for hydrogen atom transferBy similarity
    Sitei196 – 1961Allosteric effector bindingBy similarity
    Binding sitei217 – 2171Substrate; via amide nitrogenBy similarity
    Sitei226 – 2261Allosteric effector bindingBy similarity
    Active sitei397 – 3971Proton acceptorBy similarity
    Active sitei399 – 3991Cysteine radical intermediateBy similarity
    Active sitei401 – 4011Proton acceptorBy similarity
    Sitei426 – 4261Important for hydrogen atom transferBy similarity
    Sitei703 – 7031Important for electron transferBy similarity
    Sitei704 – 7041Important for electron transferBy similarity
    Sitei720 – 7201Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei723 – 7231Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. 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 subunit alpha (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase R1 subunit
    Gene namesi
    Name:nrdE
    Ordered Locus Names:Mb3077c
    OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
    Taxonomic identifieri233413 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001419: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 725725Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi189 ↔ 426Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    Induced in response to the thiol oxidant diamide.1 Publication

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    STRINGi233413.Mb3077c.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A5W9.
    SMRiP0A5W9. Positions 26-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni188 – 1892Substrate bindingBy similarity
    Regioni397 – 4015Substrate bindingBy similarity
    Regioni599 – 6035Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0209.
    HOGENOMiHOG000246165.
    KOiK00525.
    OrthoDBiEOG6J48HC.

    Family and domain databases

    InterProiIPR013346. NrdE_NrdA.
    IPR026459. RNR_1b_NrdE.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR013554. RNR_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    PF08343. RNR_N. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    TIGR04170. RNR_1b_NrdE. 1 hit.
    PROSITEiPS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A5W9-1 [UniParc]FASTAAdd to Basket

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    MPPTVIAEPV ASGAHASYSG GPGETDYHAL NAMLNLYDAD GKIQFDKDRE    50
    AAHQYFLQHV NQNTVFFHNQ DEKLDYLIRE NYYEREVLDQ YSRNFVKTLL 100
    DRAYAKKFRF PTFLGAFKYY TSYTLKTFDG KRYLERFEDR VVMVALTLAA 150
    GDTALAELLV DEIIDGRFQP ATPTFLNSGK KQRGEPVSCF LLRVEDNMES 200
    IGRSINSALQ LSKRGGGVAL LLTNIREHGA PIKNIENQSS GVIPIMKLLE 250
    DAFSYANQLG ARQGAGAVYL HAHHPDIYRF LDTKRENADE KIRIKTLSLG 300
    VVIPDITFEL AKRNDDMYLF SPYDVERVYG VPFADISVTE KYYEMVDDAR 350
    IRKTKIKARE FFQTLAELQF ESGYPYIMFE DTVNRANPID GKITHSNLCS 400
    EILQVSTPSL FNEDLSYAKV GKDISCNLGS LNIAKTMDSP DFAQTIEVAI 450
    RALTAVSDQT HIKSVPSIEQ GNNDSHAIGL GQMNLHGYLA RERIFYGSDE 500
    GIDFTNIYFY TVLYHALRAS NRIAIERGTH FKGFERSKYA SGEFFDKYTD 550
    QIWEPKTQKV RQLFADAGIR IPTQDDWRRL KESVQAHGIY NQNLQAVPPT 600
    GSISYINHST SSIHPIVSKV EIRKEGKIGR VYYPAPYMTN DNLEYYEDAY 650
    EIGYEKIIDT YAAATQHVDQ GLSLTLFFKD TATTRDVNKA QIYAWRKGIK 700
    TLYYIRLRQM ALEGTEVEGC VSCML 725
    Length:725
    Mass (Da):82,441
    Last modified:March 15, 2005 - v1
    Checksum:i38C315D149331D55
    GO

    Sequence cautioni

    The sequence CDO44346.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO44346.1. Different initiation.
    RefSeqiNP_856722.1. NC_002945.3.

    Genome annotation databases

    EnsemblBacteriaiCAD96764; CAD96764; Mb3077c.
    GeneIDi1093421.
    KEGGimbo:Mb3077c.
    PATRICi18008502. VBIMycBov88188_3381.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO44346.1 . Different initiation.
    RefSeqi NP_856722.1. NC_002945.3.

    3D structure databases

    ProteinModelPortali P0A5W9.
    SMRi P0A5W9. Positions 26-710.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 233413.Mb3077c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD96764 ; CAD96764 ; Mb3077c .
    GeneIDi 1093421.
    KEGGi mbo:Mb3077c.
    PATRICi 18008502. VBIMycBov88188_3381.

    Phylogenomic databases

    eggNOGi COG0209.
    HOGENOMi HOG000246165.
    KOi K00525.
    OrthoDBi EOG6J48HC.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR013346. NrdE_NrdA.
    IPR026459. RNR_1b_NrdE.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR013554. RNR_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    PF08343. RNR_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    TIGR04170. RNR_1b_NrdE. 1 hit.
    PROSITEi PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-935 / AF2122/97.
    2. "Thiol specific oxidative stress response in Mycobacteria."
      Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y.
      FEMS Microbiol. Lett. 249:87-94(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
      Strain: BCG / Pasteur.

    Entry informationi

    Entry nameiRIR1_MYCBO
    AccessioniPrimary (citable) accession number: P0A5W9
    Secondary accession number(s): O53296, P50640, X2BN79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome

    Documents

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

    External Data

    Dasty 3