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)

P80734

- SODN_STRSO

UniProt

P80734 - SODN_STRSO

Protein

Superoxide dismutase [Ni]

Gene

sodN

Organism
Streptomyces seoulensis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalytic activityi

    2 superoxide + 2 H+ = O2 + H2O2.

    Cofactori

    Nickel.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi15 – 151Nickel; catalytic
    Metal bindingi16 – 161Nickel; catalytic
    Metal bindingi20 – 201Nickel; catalytic

    GO - Molecular functioni

    1. nickel cation binding Source: InterPro
    2. superoxide dismutase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase

    Keywords - Ligandi

    Metal-binding, Nickel

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Ni] (EC:1.15.1.1)
    Alternative name(s):
    NiSOD
    Nickel-containing superoxide dismutase
    Gene namesi
    Name:sodN
    OrganismiStreptomyces seoulensis
    Taxonomic identifieri73044 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151H → A, C, D, K, N, Q, R, W or Y: Loss of activity. 1 Publication
    Mutagenesisi23 – 231Y → A, K or Q: Loss of activity. 1 Publication
    Mutagenesisi23 – 231Y → F or W: Slight decrease of activity. 1 Publication
    Mutagenesisi31 – 311E → A: Loss of activity. 1 Publication
    Mutagenesisi53 – 531R → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 14141 PublicationPRO_0000032908Add
    BLAST
    Chaini15 – 131117Superoxide dismutase [Ni]PRO_0000032909Add
    BLAST

    Interactioni

    Subunit structurei

    Homohexamer. The hexameric protein has roughly the shape of a hollow sphere with an outer diameter of 72 Angstroms and a large inner cavity.1 Publication

    Structurei

    Secondary structure

    1
    131
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 4419
    Helixi48 – 7427
    Helixi79 – 846
    Helixi88 – 10316
    Helixi108 – 13023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q0DX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L15-131[»]
    1Q0FX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L15-131[»]
    1Q0GX-ray1.60A/B/C/D/E/F/G/H/I/J/K/L15-131[»]
    1Q0KX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L15-131[»]
    1Q0MX-ray1.68A/B/C/D/E/F15-131[»]
    ProteinModelPortaliP80734.
    SMRiP80734. Positions 15-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80734.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the nickel superoxide dismutase family.Curated

    Family and domain databases

    Gene3Di1.20.120.400. 1 hit.
    InterProiIPR014123. Superoxide_dismutase_Ni-type.
    [Graphical view]
    PfamiPF09055. Sod_Ni. 1 hit.
    [Graphical view]
    SUPFAMiSSF109770. SSF109770. 1 hit.
    TIGRFAMsiTIGR02753. sodN. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P80734-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSRLFAPKV KVSAHCDLPC GVYDPAQARI EAESVKAIQE KMAANDDLHF    50
    QIRATVIKEQ RAELAKHHLD VLWSDYFKPP HFESYPELHT LVNEAVKALS 100
    AAKASTDPAT GQKALDYIAQ IDKIFWETKK A 131
    Length:131
    Mass (Da):14,717
    Last modified:December 1, 2000 - v2
    Checksum:iDD5467214689478C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161C → G AA sequence (PubMed:8836134)Curated
    Sequence conflicti20 – 201C → G AA sequence (PubMed:8836134)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047528 Genomic DNA. Translation: AAD17486.1.
    AF047461 Genomic DNA. Translation: AAD17482.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047528 Genomic DNA. Translation: AAD17486.1 .
    AF047461 Genomic DNA. Translation: AAD17482.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q0D X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 15-131 [» ]
    1Q0F X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 15-131 [» ]
    1Q0G X-ray 1.60 A/B/C/D/E/F/G/H/I/J/K/L 15-131 [» ]
    1Q0K X-ray 2.10 A/B/C/D/E/F/G/H/I/J/K/L 15-131 [» ]
    1Q0M X-ray 1.68 A/B/C/D/E/F 15-131 [» ]
    ProteinModelPortali P80734.
    SMRi P80734. Positions 15-131.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P80734.

    Family and domain databases

    Gene3Di 1.20.120.400. 1 hit.
    InterProi IPR014123. Superoxide_dismutase_Ni-type.
    [Graphical view ]
    Pfami PF09055. Sod_Ni. 1 hit.
    [Graphical view ]
    SUPFAMi SSF109770. SSF109770. 1 hit.
    TIGRFAMsi TIGR02753. sodN. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of sodN encoding Ni-containing superoxide dismutase from Streptomyces seoulensis."
      Kang S.-O., Yim Y.I., Youn H.-D.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: IMSNU-1.
    2. "A novel nickel-containing superoxide dismutase from Streptomyces spp."
      Youn H.-D., Kim E.-J., Roe J.-H., Hah Y.C., Kang S.-O.
      Biochem. J. 318:889-896(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 15-28.
      Strain: IMSNU-1.
    3. "Crystal structure of nickel-containing superoxide dismutase reveals another type of active site."
      Wuerges J., Lee J.W., Yim Y.I., Yim H.S., Kang S.O., Carugo K.D.
      Proc. Natl. Acad. Sci. U.S.A. 101:8569-8574(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 15-131 IN COMPLEX WITH NICKEL IONS, MUTAGENESIS OF HIS-15; TYR-23; GLU-31 AND ARG-53, SUBUNIT.

    Entry informationi

    Entry nameiSODN_STRSO
    AccessioniPrimary (citable) accession number: P80734
    Secondary accession number(s): Q9Z368
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 66 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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3