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P50621

- RIR2_BACSU

UniProt

P50621 - RIR2_BACSU

Protein

Ribonucleoside-diphosphate reductase subunit beta

Gene

nrdF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.PROSITE-ProRule annotation

    Cofactori

    Binds 2 iron ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi66 – 661Iron 1PROSITE-ProRule annotation
    Metal bindingi97 – 971Iron 1PROSITE-ProRule annotation
    Metal bindingi97 – 971Iron 2By similarity
    Metal bindingi101 – 1011Iron 1PROSITE-ProRule annotation
    Active sitei105 – 1051PROSITE-ProRule annotation
    Metal bindingi164 – 1641Iron 2By similarity
    Metal bindingi198 – 1981Iron 2By similarity
    Metal bindingi201 – 2011Iron 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. deoxyribonucleotide biosynthetic process Source: InterPro
    3. DNA replication Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU17390-MONOMER.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase subunit beta (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase small subunit
    Gene namesi
    Name:nrdF
    Ordered Locus Names:BSU17390
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU17390. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Ribonucleoside-diphosphate reductase subunit betaPRO_0000190469Add
    BLAST

    Proteomic databases

    PaxDbiP50621.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    STRINGi224308.BSU17390.

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123
    Beta strandi14 – 174
    Helixi18 – 2710
    Helixi32 – 343
    Helixi38 – 403
    Helixi41 – 455
    Helixi49 – 7123
    Helixi73 – 808
    Helixi84 – 9916
    Helixi101 – 11212
    Helixi115 – 12713
    Helixi129 – 14315
    Helixi150 – 16516
    Turni166 – 1683
    Helixi169 – 17911
    Turni180 – 1823
    Helixi185 – 21329
    Helixi218 – 24730
    Helixi248 – 2503
    Helixi253 – 27018
    Helixi284 – 2885

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DR0X-ray1.90A/B1-329[»]
    ProteinModelPortaliP50621.
    SMRiP50621. Positions 4-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0208.
    HOGENOMiHOG000246154.
    KOiK00526.
    OMAiEVGWTEE.
    OrthoDBiEOG68DD19.
    PhylomeDBiP50621.

    Family and domain databases

    Gene3Di1.10.620.20. 1 hit.
    InterProiIPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR026023. RNR_bsu_prok.
    IPR026494. RNR_NrdF.
    IPR000358. RNR_small.
    [Graphical view]
    PANTHERiPTHR23409. PTHR23409. 1 hit.
    PfamiPF00268. Ribonuc_red_sm. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000355. NrdB. 1 hit.
    SUPFAMiSSF47240. SSF47240. 1 hit.
    TIGRFAMsiTIGR04171. RNR_1b_NrdF. 1 hit.
    PROSITEiPS00368. RIBORED_SMALL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50621-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKIYDAANW SKHEDDFTQM FYNQNVKQFW LPEEIALNGD LLTWKYLGKN    50
    EQDTYMKVLA GLTLLDTEQG NTGMPIVAEH VDGHQRKAVL NFMAMMENAV 100
    HAKSYSNIFM TLAPTETINE VFEWVKQNKY LQKKAQMIVG LYKAIQKDDE 150
    ISLFKAMVAS VYLESFLFYS GFYYPLYFYG QGKLMQSGEI INLILRDEAI 200
    HGVYVGLLAQ EIYNKQTEEK KAELREFAID LLNQLYENEL EYTEDLYDQV 250
    GLSHDVKKFI RYNANKALMN LGFDPYFEEE DINPIVLNGL NTKTKSHDFF 300
    SMKGNGYKKA TVEPLKDDDF YFEDEKEQI 329
    Length:329
    Mass (Da):38,379
    Last modified:October 1, 1996 - v1
    Checksum:i5080C014D2868EEB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z68500 Genomic DNA. Translation: CAA92811.1.
    AL009126 Genomic DNA. Translation: CAB13623.1.
    PIRiC69667.
    RefSeqiNP_389621.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13623; CAB13623; BSU17390.
    GeneIDi940076.
    KEGGibsu:BSU17390.
    PATRICi18975289. VBIBacSub10457_1836.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z68500 Genomic DNA. Translation: CAA92811.1 .
    AL009126 Genomic DNA. Translation: CAB13623.1 .
    PIRi C69667.
    RefSeqi NP_389621.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DR0 X-ray 1.90 A/B 1-329 [» ]
    ProteinModelPortali P50621.
    SMRi P50621. Positions 4-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU17390.

    Proteomic databases

    PaxDbi P50621.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13623 ; CAB13623 ; BSU17390 .
    GeneIDi 940076.
    KEGGi bsu:BSU17390.
    PATRICi 18975289. VBIBacSub10457_1836.

    Organism-specific databases

    GenoListi BSU17390. [Micado ]

    Phylogenomic databases

    eggNOGi COG0208.
    HOGENOMi HOG000246154.
    KOi K00526.
    OMAi EVGWTEE.
    OrthoDBi EOG68DD19.
    PhylomeDBi P50621.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci BSUB:BSU17390-MONOMER.

    Family and domain databases

    Gene3Di 1.10.620.20. 1 hit.
    InterProi IPR009078. Ferritin-like_SF.
    IPR012348. RNR-rel.
    IPR026023. RNR_bsu_prok.
    IPR026494. RNR_NrdF.
    IPR000358. RNR_small.
    [Graphical view ]
    PANTHERi PTHR23409. PTHR23409. 1 hit.
    Pfami PF00268. Ribonuc_red_sm. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000355. NrdB. 1 hit.
    SUPFAMi SSF47240. SSF47240. 1 hit.
    TIGRFAMsi TIGR04171. RNR_1b_NrdF. 1 hit.
    PROSITEi PS00368. RIBORED_SMALL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Bacillus subtilis genes for ribonucleotide reductase are similar to the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae."
      Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M.
      Microbiology 142:2995-3004(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.

    Entry informationi

    Entry nameiRIR2_BACSU
    AccessioniPrimary (citable) accession number: P50621
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 106 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3