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Reviewed, UniProtKB/Swiss-Prot Q9Y8D9 (SODC_ASPFU)

Last modified September 22, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Superoxide dismutase [Cu-Zn]
    EC=1.15.1.1
Gene names
Name: sodC
ORF Names: AFUA_5G09240
OrganismAspergillus fumigatus (Sartorya fumigata) [Complete proteome]
Taxonomic identifier5085 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Sequence caution

The sequence EAL91677.1 differs from that shown. Reason: Erroneous gene model prediction.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionantioxidant activity

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 154153Superoxide dismutase [Cu-Zn]
PRO_0000164108

Sites

Metal binding471Copper By similarity
Metal binding491Copper By similarity
Metal binding641Copper By similarity
Metal binding641Zinc By similarity
Metal binding721Zinc By similarity
Metal binding811Zinc By similarity
Metal binding841Zinc By similarity
Metal binding1211Copper By similarity

Amino acid modifications

Disulfide bond58 ↔ 147 By similarity

Experimental info

Sequence conflict81Missing in AAL38991. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9Y8D9-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FB2FC504140DDED6

FASTA15415,967
        10         20         30         40         50         60 
MVKAVAVLRG DSKITGTVTF EQADENSPTT VSWNIKGNDP NAKRGFHVHQ FGDNTNGCTS 

        70         80         90        100        110        120 
AGPHFNPYGK THGAPEDSER HVGDLGNFET DAEGNAVGSK QDKLIKLIGA ESVLGRTLVV 

       130        140        150 
HAGTDDLGRG GNEESKKTGN AGARPACGVI GIAA

« Hide

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References

« Hide 'large scale' references
[1]"Production and characterization of recombinant Aspergillus fumigatus Cu,Zn superoxide dismutase and its recognition by immune human sera."
Holdom M.D., Lechenne B., Hay R.J., Hamilton A.J., Monod M.
J. Clin. Microbiol. 38:558-562(2000) [PubMed: 10655345] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Homogeneity in 3-dimensional structure of Cu,Zn superoxide dismutases of Aspergillus fumigatus, Aspergillus flavus and Aspergillus nidulans."
Holdom M.D., Hobby P., Lechenne B., Zaugg C., Sutton B., Monod M., Hamilton A.J.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Af293 / CBS 101355 / FGSC A1100.

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Cross-references

Sequence databases

AF128886 mRNA. Translation: AAD42060.1.
AF281057 Genomic DNA. Translation: AAL38991.1.
AAHF01000003 Genomic DNA. Translation: EAL91677.1. Sequence problems.
RefSeqXP_753715.1.

3D structure databases

HSSPHSSP built from PDB template 1OZU based on UniProtKB P00441.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9Y8D9.

Genome annotation databases

GeneID3511006.
GenomeReviewsGene locus sodC in contig CM000173_GR.
KEGGafm:AFUA_5G09240.

Phylogenomic databases

HOGENOMQ9Y8D9.

Enzyme and pathway databases

BRENDA1.15.1.1. 18841.

Family and domain databases

InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
ProDomPD000469. SOD_CU_ZN. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSODC_ASPFU
AccessionPrimary (citable) accession number: Q9Y8D9
Secondary accession number(s): Q4WUP9, Q8X1S8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2007
Last modified: September 22, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents