Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Superoxide dismutase [Ni]

Gene

sodN

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

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
Complete GO annotation...

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
Synonyms:sod1
Ordered Locus Names:SCO5254
ORF Names:2SC7G11.16c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 14142 PublicationsPRO_0000032906Add
BLAST
Chaini15 – 131117Superoxide dismutase [Ni]PRO_0000032907Add
BLAST

Proteomic databases

PRIDEiP80735.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

STRINGi100226.SCO5254.

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Helixi26 – 4419Combined sources
Helixi48 – 7528Combined sources
Helixi79 – 846Combined sources
Helixi88 – 10316Combined sources
Helixi108 – 12821Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP80735.
SMRiP80735. Positions 15-131.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80735.

Family & Domainsi

Sequence similaritiesi

Belongs to the nickel superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiNOG39351.
HOGENOMiHOG000020289.
KOiK00518.
OMAiWTDYFKP.
OrthoDBiEOG683S9W.

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.

P80735-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSRLFAPKV TVSAHCDLPC GVYDPAQARI EAESVKAVQE KMAGNDDPHF
60 70 80 90 100
QTRATVIKEQ RAELAKHHVS VLWSDYFKPP HFEKYPELHQ LVNDTLKALS
110 120 130
AAKGSKDPAT GQKALDYIAQ IDKIFWETKK A
Length:131
Mass (Da):14,703
Last modified:December 1, 2000 - v2
Checksum:i8DA21AFBAC0D7EF6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161C → G AA sequence (PubMed:8836134)Curated
Sequence conflicti16 – 161C → G AA sequence (PubMed:8898904)Curated
Sequence conflicti20 – 201C → G AA sequence (PubMed:8836134)Curated
Sequence conflicti20 – 201C → G AA sequence (PubMed:8898904)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012193 Genomic DNA. Translation: AAC38082.1.
AF104994 Genomic DNA. Translation: AAF25537.1.
AL939123 Genomic DNA. Translation: CAC05965.1.
RefSeqiNP_629400.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAC05965; CAC05965; CAC05965.
GeneIDi1100695.
KEGGisco:SCO5254.
PATRICi23740360. VBIStrCoe124346_5338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012193 Genomic DNA. Translation: AAC38082.1.
AF104994 Genomic DNA. Translation: AAF25537.1.
AL939123 Genomic DNA. Translation: CAC05965.1.
RefSeqiNP_629400.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP80735.
SMRiP80735. Positions 15-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO5254.

Proteomic databases

PRIDEiP80735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC05965; CAC05965; CAC05965.
GeneIDi1100695.
KEGGisco:SCO5254.
PATRICi23740360. VBIStrCoe124346_5338.

Phylogenomic databases

eggNOGiNOG39351.
HOGENOMiHOG000020289.
KOiK00518.
OMAiWTDYFKP.
OrthoDBiEOG683S9W.

Miscellaneous databases

EvolutionaryTraceiP80735.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 15-131 IN COMPLEX WITH NICKEL IONS, SUBUNIT.

Entry informationi

Entry nameiSODN_STRCO
AccessioniPrimary (citable) accession number: P80735
Secondary accession number(s): O51921
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: January 7, 2015
This is version 96 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, Complete proteome, Direct protein sequencing, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.