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P80734 (SODN_STRSO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Ni]
EC=1.15.1.1
Alternative name(s):
NiSOD
Nickel-containing superoxide dismutase
Gene names
Name:sodN
OrganismStreptomyces seoulensis
Taxonomic identifier73044 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Nickel.

Subunit structure

Homohexamer. The hexameric protein has roughly the shape of a hollow sphere with an outer diameter of 72 Angstroms and a large inner cavity. Ref.3

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the nickel superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionAntioxidant
Oxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnickel cation binding

Inferred from electronic annotation. Source: InterPro

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1414
PRO_0000032908
Chain15 – 131117Superoxide dismutase [Ni]
PRO_0000032909

Sites

Metal binding151Nickel; catalytic
Metal binding161Nickel; catalytic
Metal binding201Nickel; catalytic

Experimental info

Mutagenesis151H → A, C, D, K, N, Q, R, W or Y: Loss of activity. Ref.3
Mutagenesis231Y → A, K or Q: Loss of activity. Ref.3
Mutagenesis231Y → F or W: Slight decrease of activity. Ref.3
Mutagenesis311E → A: Loss of activity. Ref.3
Mutagenesis531R → A: Loss of activity. Ref.3
Sequence conflict161C → G AA sequence Ref.2
Sequence conflict201C → G AA sequence Ref.2

Secondary structure

1 ........... 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80734 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: DD5467214689478C

FASTA13114,717
        10         20         30         40         50         60 
MLSRLFAPKV KVSAHCDLPC GVYDPAQARI EAESVKAIQE KMAANDDLHF QIRATVIKEQ 

        70         80         90        100        110        120 
RAELAKHHLD VLWSDYFKPP HFESYPELHT LVNEAVKALS AAKASTDPAT GQKALDYIAQ 

       130 
IDKIFWETKK A

« Hide

References

[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: 8836134] [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: 15173586] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF047528 Genomic DNA. Translation: AAD17486.1.
AF047461 Genomic DNA. Translation: AAD17482.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP80734.
SMRP80734. Positions 15-131.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR014123. Superoxide_dismutase_Ni-type.
[Graphical view]
Gene3DG3DSA:1.20.120.400. Superoxide_dismutase_Ni-type. 1 hit.
PfamPF09055. Sod_Ni. 1 hit.
[Graphical view]
SUPFAMSSF109770. Superoxide_dismutase_Ni-type. 1 hit.
TIGRFAMsTIGR02753. SodN. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSODN_STRSO
AccessionPrimary (citable) accession number: P80734
Secondary accession number(s): Q9Z368
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: June 28, 2011
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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