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P80735 (SODN_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:sod1
Ordered Locus Names:SCO5254
ORF Names:2SC7G11.16c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

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 a roughly the shape of a hollow sphere with an outer diameter of 60 angstroms and a large interior cavity. Ref.5

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
Complete proteome
Direct protein sequencing
Reference proteome
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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1414
PRO_0000032906
Chain15 – 131117Superoxide dismutase [Ni]
PRO_0000032907

Sites

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

Experimental info

Sequence conflict161C → G AA sequence Ref.3
Sequence conflict161C → G AA sequence Ref.4
Sequence conflict201C → G AA sequence Ref.3
Sequence conflict201C → G AA sequence Ref.4

Secondary structure

............. 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80735 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 8DA21AFBAC0D7EF6

FASTA13114,703
        10         20         30         40         50         60 
MLSRLFAPKV TVSAHCDLPC GVYDPAQARI EAESVKAVQE KMAGNDDPHF QTRATVIKEQ 

        70         80         90        100        110        120 
RAELAKHHVS VLWSDYFKPP HFEKYPELHQ LVNDTLKALS AAKGSKDPAT GQKALDYIAQ 

       130 
IDKIFWETKK A 

« Hide

References

« Hide 'large scale' references
[1]"Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller."
Kim E.-J., Chung H.-J., Suh B., Hah Y.C., Roe J.-H.
Mol. Microbiol. 27:187-195(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020 and ATCC BAA-471 / A3(2) / M145.
[2]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[3]"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: ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020.
[4]"Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor."
Kim F.-J., Kim H.-P., Hah Y.V., Roe J.-H.
Eur. J. Biochem. 241:178-185(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-28.
Strain: ATCC 10147 / DSM 41007 / JCM 4020 / NBRC 3176 / KCC S-0020.
[5]"Nickel superoxide dismutase structure and mechanism."
Barondeau D.P., Kassmann C.J., Bruns C.K., Tainer J.A., Getzoff E.D.
Biochemistry 43:8038-8047(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 15-131 IN COMPLEX WITH NICKEL IONS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF012193 Genomic DNA. Translation: AAC38082.1.
AF104994 Genomic DNA. Translation: AAF25537.1.
AL939123 Genomic DNA. Translation: CAC05965.1.
RefSeqNP_629400.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T6IX-ray2.81A/B/C15-131[»]
1T6QX-ray2.05A/B/C15-131[»]
1T6UX-ray1.30A/B/C/D/E/F/G/H/I/J/K/L15-131[»]
3G4XX-ray2.01A/B/C15-131[»]
3G4ZX-ray1.87A/B/C15-131[»]
3G50X-ray1.90A/B/C15-131[»]
ProteinModelPortalP80735.
SMRP80735. Positions 15-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO5254.

Proteomic databases

PRIDEP80735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC05965; CAC05965; CAC05965.
GeneID1100695.
KEGGsco:SCO5254.
PATRIC23740360. VBIStrCoe124346_5338.

Phylogenomic databases

eggNOGNOG39351.
HOGENOMHOG000020289.
KOK00518.
OMAWTDYFKP.
OrthoDBEOG683S9W.
ProtClustDBCLSK902881.

Family and domain databases

Gene3D1.20.120.400. 1 hit.
InterProIPR014123. Superoxide_dismutase_Ni-type.
[Graphical view]
PfamPF09055. Sod_Ni. 1 hit.
[Graphical view]
SUPFAMSSF109770. SSF109770. 1 hit.
TIGRFAMsTIGR02753. sodN. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP80735.

Entry information

Entry nameSODN_STRCO
AccessionPrimary (citable) accession number: P80735
Secondary accession number(s): O51921
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: November 13, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references