Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9CBQ0

- RIR1_MYCLE

UniProt

Q9CBQ0 - RIR1_MYCLE

Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdE

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (29 Aug 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei168 – 1681SubstrateBy similarity
    Sitei185 – 1851Important for hydrogen atom transferBy similarity
    Sitei192 – 1921Allosteric effector bindingBy similarity
    Binding sitei213 – 2131Substrate; via amide nitrogenBy similarity
    Sitei222 – 2221Allosteric effector bindingBy similarity
    Active sitei393 – 3931Proton acceptorBy similarity
    Active sitei395 – 3951Cysteine radical intermediateBy similarity
    Active sitei397 – 3971Proton acceptorBy similarity
    Sitei422 – 4221Important for hydrogen atom transferBy similarity
    Sitei699 – 6991Important for electron transferBy similarity
    Sitei700 – 7001Important for electron transferBy similarity
    Sitei716 – 7161Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei719 – 7191Interacts 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:ML1734
    OrganismiMycobacterium leprae (strain TN)
    Taxonomic identifieri272631 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000806: Chromosome

    Organism-specific databases

    LepromaiML1734.

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 721721Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187220Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi185 ↔ 422Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    STRINGi272631.ML1734.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CBQ0.
    SMRiQ9CBQ0. Positions 16-706.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 1852Substrate bindingBy similarity
    Regioni393 – 3975Substrate bindingBy similarity
    Regioni595 – 5995Substrate 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.

    Q9CBQ0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPTATAEPV TASTHMLSNE TDYHALNAML NLYDADGKIQ FDKDVLAARQ    50
    FFLQHVNQNT VFFHNQDEKL DYLIRENYYE REVLDQYSRN FVKSLLDRAY 100
    AKKFRFSTFL GAFKYYTSYT LKTFDGKRYL ERLEDRVCMV ALTLAAGDTG 150
    LAEKLVDEII DGRFQPATPT FLNSGKKQRG EPVSCFLLRI EDNMESIGRS 200
    VNSALQLSKR GGGVALLLSN IREHGAPIKN IEHQSSGVIP IMKLLEDAFS 250
    YANQLGARQG AGAVYLHAHH PDIYRFLDTK RENADEKIRI KTLSLGVIIP 300
    DITFELAKRN EDMYLFSSYD VERVYEVPFA DISVTEKYYE MLDDARIRKT 350
    KIKAREFFQK LAELQFESGY PYVMFEDTVN RANPIEGKIT HSNLCSEILQ 400
    VSTPSLFNDD LSYAKVGKDI SCNLGSLNIA KTMDSPDFAQ TVEVAIRALT 450
    AVSDQTHIKS VPSIEQGNND SHAIGLGQMN LHGYLSREGI FYGSEEGVDF 500
    TNIYFYTVLF HVLLASNSIA IERGTFFKGF ERSKYASGEF FDKYIEQTWE 550
    PKTDKVRQLF AEAAIRIPTQ NDWKRLKELV VAHGIYNQNL QAVPPTGSIS 600
    YINHSTSSIH PIVSKVEIRK EGKIGRVYYP APYMTNDNLQ YYQDAYEIGY 650
    QKIIDTYAAA TQHVDQGLSL TLFFKDTATT RDVNKAQIYA WRKGIKTLYY 700
    IRLRQMALEG TEVEGCVSCT L 721
    Length:721
    Mass (Da):82,024
    Last modified:August 29, 2001 - v2
    Checksum:i22B365A016228872
    GO

    Sequence cautioni

    The sequence CAC30687.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL583923 Genomic DNA. Translation: CAC30687.1. Different initiation.
    PIRiH87125.
    RefSeqiNP_302195.1. NC_002677.1.

    Genome annotation databases

    EnsemblBacteriaiCAC30687; CAC30687; CAC30687.
    GeneIDi910759.
    KEGGimle:ML1734.
    PATRICi18056662. VBIMycLep78757_3260.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL583923 Genomic DNA. Translation: CAC30687.1 . Different initiation.
    PIRi H87125.
    RefSeqi NP_302195.1. NC_002677.1.

    3D structure databases

    ProteinModelPortali Q9CBQ0.
    SMRi Q9CBQ0. Positions 16-706.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272631.ML1734.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC30687 ; CAC30687 ; CAC30687 .
    GeneIDi 910759.
    KEGGi mle:ML1734.
    PATRICi 18056662. VBIMycLep78757_3260.

    Organism-specific databases

    Lepromai ML1734.

    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: TN.

    Entry informationi

    Entry nameiRIR1_MYCLE
    AccessioniPrimary (citable) accession number: Q9CBQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: August 29, 2001
    Last modified: October 1, 2014
    This is version 81 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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