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P69925

- RIR2_ECO57

UniProt

P69925 - RIR2_ECO57

Protein

Ribonucleoside-diphosphate reductase 1 subunit beta

Gene

nrdB

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.PROSITE-ProRule annotation

    Cofactori

    Binds 2 iron ions per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi85 – 851Iron 1PROSITE-ProRule annotation
    Metal bindingi116 – 1161Iron 1PROSITE-ProRule annotation
    Metal bindingi116 – 1161Iron 2By similarity
    Metal bindingi119 – 1191Iron 1PROSITE-ProRule annotation
    Active sitei123 – 1231PROSITE-ProRule annotation
    Metal bindingi205 – 2051Iron 2By similarity
    Metal bindingi239 – 2391Iron 2By similarity
    Metal bindingi242 – 2421Iron 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
    2. DNA replication Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciECOL386585:GJFA-3070-MONOMER.
    ECOO157:NRDB-MONOMER.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase 1 subunit beta (EC:1.17.4.1)
    Alternative name(s):
    Protein B2
    Protein R2
    Ribonucleotide reductase 1
    Gene namesi
    Name:nrdB
    Synonyms:ftsB
    Ordered Locus Names:Z3491, ECs3118
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 376375Ribonucleoside-diphosphate reductase 1 subunit betaPRO_0000190477Add
    BLAST

    Proteomic databases

    PRIDEiP69925.

    Interactioni

    Subunit structurei

    Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 protein is a dimer of alpha subunits. A radical transfer pathway occurs between Tyr-123 of R2 and R1 By similarity.By similarity

    Protein-protein interaction databases

    MINTiMINT-1233701.
    STRINGi155864.Z3491.

    Structurei

    3D structure databases

    ProteinModelPortaliP69925.
    SMRiP69925. Positions 2-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0208.
    HOGENOMiHOG000278087.
    KOiK00526.
    OMAiWIETWAF.
    OrthoDBiEOG6J48J7.

    Family and domain databases

    Gene3Di1.10.620.20. 1 hit.
    InterProiIPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR000358. RNR_small.
    [Graphical view]
    PANTHERiPTHR23409. PTHR23409. 1 hit.
    PfamiPF00268. Ribonuc_red_sm. 2 hits.
    [Graphical view]
    SUPFAMiSSF47240. SSF47240. 1 hit.
    PROSITEiPS00368. RIBORED_SMALL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P69925-1 [UniParc]FASTAAdd to Basket

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    MAYTTFSQTK NDQLKEPMFF GQPVNVARYD QQKYDIFEKL IEKQLSFFWR    50
    PEEVDVSRDR IDYQALPEHE KHIFISNLKY QTLLDSIQGR SPNVALLPLI 100
    SIPELETWVE TWAFSETIHS RSYTHIIRNI VNDPSVVFDD IVTNEQIQKR 150
    AEGISSYYDE LIEMTSYWHL LGEGTHTVNG KTVTVSLREL KKKLYLCLMS 200
    VNALEAIRFY VSFACSFAFA ERELMEGNAK IIRLIARDEA LHLTGTQHML 250
    NLLRSGADDP EMAEIAEECK QECYDLFVQA AQQEKDWADY LFRDGSMIGL 300
    NKDILCQYVE YITNIRMQAV GLDLPFQTRS NPIPWINTWL VSDNVQVAPQ 350
    EVEVSSYLVG QIDSEVDTDD LSNFQL 376
    Length:376
    Mass (Da):43,517
    Last modified:January 23, 2007 - v2
    Checksum:iBF2D9A49B643E84A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG57364.1.
    BA000007 Genomic DNA. Translation: BAB36541.1.
    PIRiF91018.
    H85862.
    RefSeqiNP_288809.1. NC_002655.2.
    NP_311145.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG57364; AAG57364; Z3491.
    BAB36541; BAB36541; BAB36541.
    GeneIDi916826.
    957218.
    KEGGiece:Z3491.
    ecs:ECs3118.
    PATRICi18355620. VBIEscCol44059_3011.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG57364.1 .
    BA000007 Genomic DNA. Translation: BAB36541.1 .
    PIRi F91018.
    H85862.
    RefSeqi NP_288809.1. NC_002655.2.
    NP_311145.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali P69925.
    SMRi P69925. Positions 2-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1233701.
    STRINGi 155864.Z3491.

    Proteomic databases

    PRIDEi P69925.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG57364 ; AAG57364 ; Z3491 .
    BAB36541 ; BAB36541 ; BAB36541 .
    GeneIDi 916826.
    957218.
    KEGGi ece:Z3491.
    ecs:ECs3118.
    PATRICi 18355620. VBIEscCol44059_3011.

    Phylogenomic databases

    eggNOGi COG0208.
    HOGENOMi HOG000278087.
    KOi K00526.
    OMAi WIETWAF.
    OrthoDBi EOG6J48J7.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci ECOL386585:GJFA-3070-MONOMER.
    ECOO157:NRDB-MONOMER.

    Family and domain databases

    Gene3Di 1.10.620.20. 1 hit.
    InterProi IPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR000358. RNR_small.
    [Graphical view ]
    PANTHERi PTHR23409. PTHR23409. 1 hit.
    Pfami PF00268. Ribonuc_red_sm. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47240. SSF47240. 1 hit.
    PROSITEi PS00368. RIBORED_SMALL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiRIR2_ECO57
    AccessioniPrimary (citable) accession number: P69925
    Secondary accession number(s): P00453
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    E.coli produces two separate class I enzymes. This one is the functional enzyme during growth.
    A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2.By similarity

    Keywords - Technical termi

    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