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Q3MSU9 (SODB_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Mn], mitochondrial
EC=1.15.1.1
Gene names
Name:sodB
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems By similarity.

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 manganese ion per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion By similarity
Chain? – 210Superoxide dismutase [Mn], mitochondrialPRO_0000043335

Sites

Metal binding291Manganese By similarity
Metal binding771Manganese By similarity
Metal binding1641Manganese By similarity
Metal binding1681Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MSU9 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 41FA2D7450CCC1FB

FASTA21023,693
        10         20         30         40         50         60 
MTSKCTLPDL PYDYDALEPI ISKQIMELHH KKHHQTYVNN LNAALASQAS ALDSNDITQL 

        70         80         90        100        110        120 
ISIQQKLKFN GGGHINHSLF WKNLARYDSP ATNLERSAPS LKDAIEKQWG SVKNFTDAFE 

       130        140        150        160        170        180 
AVLLGIQGSG WGWLVSSGKT GFLEIVTTKD QDPVTGPIPV FGVDMWEHAY YLQYLNNKAS 

       190        200        210 
YVQNIWKVIN WEEAEHRYLN GTEELGSLKL

« Hide

References

[1]"UPR-independent dithiothreitol stress-induced genes in Aspergillus niger."
MacKenzie D.A., Guillemette T., Al-Sheikh H., Watson A.J., Jeenes D.J., Wongwathanarat P., Dunn-Coleman N.S., van Peij N., Archer D.B.
Mol. Genet. Genomics 274:410-418(2005) [PubMed: 16160852] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ812006 Genomic DNA. Translation: CAH19233.1.

3D structure databases

ProteinModelPortalQ3MSU9.
SMRQ3MSU9. Positions 6-201.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3MSU9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

PhylomeDBQ3MSU9.

Family and domain databases

InterProIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERPTHR11404. SODismutase. 1 hit.
PfamPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFPIRSF000349. SODismutase. 1 hit.
PRINTSPR01703. MNSODISMTASE.
SUPFAMSSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.
PROSITEPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODB_ASPNG
AccessionPrimary (citable) accession number: Q3MSU9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 25, 2005
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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