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F0MR64

- F0MR64_NEIMM

UniProt

F0MR64 - F0MR64_NEIMM

Protein

Superoxide dismutase [Cu-Zn]

Gene

NMBM01240149_0758

Organism
Neisseria meningitidis serogroup B (strain M01-240149)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 18 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      Previous versions | rss
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    Functioni

    Destroys radicals which are normally produced within the cells and which are toxic to biological systems.UniRule annotation

    Catalytic activityi

    2 superoxide + 2 H+ = O2 + H2O2.UniRule annotation

    Cofactori

    Binds 1 copper ion per subunit.UniRule annotation
    Binds 1 zinc ion per subunit.UniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. superoxide dismutase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    OxidoreductaseUniRule annotation

    Keywords - Ligandi

    CopperUniRule annotation, Metal-bindingUniRule annotation, ZincUniRule annotation

    Enzyme and pathway databases

    BioCyciNMEN935591:GLHR-757-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Cu-Zn]UniRule annotation (EC:1.15.1.1UniRule annotation)
    Gene namesi
    Ordered Locus Names:NMBM01240149_0758Imported
    OrganismiNeisseria meningitidis serogroup B (strain M01-240149)Imported
    Taxonomic identifieri935591 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000007480: Chromosome

    Structurei

    3D structure databases

    ProteinModelPortaliF0MR64.
    SMRiF0MR64. Positions 32-186.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.UniRule annotation

    Phylogenomic databases

    KOiK04565.
    OMAiDHPKPLG.

    Family and domain databases

    Gene3Di2.60.40.200. 1 hit.
    InterProiIPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view]
    PfamiPF00080. Sod_Cu. 1 hit.
    [Graphical view]
    SUPFAMiSSF49329. SSF49329. 1 hit.
    PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    F0MR64-1 [UniParc]FASTAAdd to Basket

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    MNMKTLLALA VSAVCSVGVA QAHEHNTIPK GASIEVKVQQ LDPVNGNKDV    50
    GTVTITESNY GLVFTPDLQG LSEGLHGFHI HENPSCEPKE KEGKLTAGLG 100
    AGGHWDPKGA KQHGYPWQDD AHLGDLPALT VLHDGTATNP VLAPRLKHLD 150
    DVRGHSIMIH TGGDNHSDHP APLGGGGPRM ACGVIK 186
    Length:186
    Mass (Da):19,520
    Last modified:May 3, 2011 - v1
    Checksum:i6499049BFAC3427C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002421 Genomic DNA. Translation: ADY97349.1.
    RefSeqiYP_005895560.1. NC_017514.1.

    Genome annotation databases

    EnsemblBacteriaiADY97349; ADY97349; NMBM01240149_0758.
    GeneIDi12412438.
    KEGGinmm:NMBM01240149_0758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002421 Genomic DNA. Translation: ADY97349.1 .
    RefSeqi YP_005895560.1. NC_017514.1.

    3D structure databases

    ProteinModelPortali F0MR64.
    SMRi F0MR64. Positions 32-186.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADY97349 ; ADY97349 ; NMBM01240149_0758 .
    GeneIDi 12412438.
    KEGGi nmm:NMBM01240149_0758.

    Phylogenomic databases

    KOi K04565.
    OMAi DHPKPLG.

    Enzyme and pathway databases

    BioCyci NMEN935591:GLHR-757-MONOMER.

    Family and domain databases

    Gene3Di 2.60.40.200. 1 hit.
    InterProi IPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view ]
    Pfami PF00080. Sod_Cu. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49329. SSF49329. 1 hit.
    PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Neisseria meningitidis is structured in clades associated with restriction modification systems that modulate homologous recombination."
      Budroni S., Siena E., Hotopp J.C., Seib K.L., Serruto D., Nofroni C., Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A., Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.
      Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: M01-240149Imported.

    Entry informationi

    Entry nameiF0MR64_NEIMM
    AccessioniPrimary (citable) accession number: F0MR64
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 3, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 18 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3