Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q92450 (SODM_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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 [Mn], mitochondrial
EC=1.15.1.1
Alternative name(s):
Allergen=Asp f 6
Gene names
Name:sodB
ORF Names:AFUA_1G14550
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifier330879 [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 existenceEvidence at protein level

General annotation (Comments)

Function

Destroys superoxide anion 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 manganese ion per subunit.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Belongs to the iron/manganese superoxide dismutase family.

Sequence caution

The sequence AAB60779.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   DiseaseAllergen
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
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_0000032881

Sites

Metal binding291Manganese
Metal binding771Manganese
Metal binding1631Manganese
Metal binding1671Manganese

Experimental info

Sequence conflict551N → T in AAB60779. Ref.1

Secondary structure

1 ................................ 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92450 [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: CE701E7086E414FC

FASTA21023,390
        10         20         30         40         50         60 
MSQQYTLPPL PYPYDALQPY ISQQIMELHH KKHHQTYVNG LNAALEAQKK AAEANDVPKL 

        70         80         90        100        110        120 
VSVQQAIKFN GGGHINHSLF WKNLAPEKSG GGKIDQAPVL KAAIEQRWGS FDKFKDAFNT 

       130        140        150        160        170        180 
TLLGIQGSGW GWLVTDGPKG KLDITTTHDQ DPVTGAAPVF GVDMWEHAYY LQYLNDKASY 

       190        200        210 
AKGIWNVINW AEAENRYIAG DKGGHPFMKL

« Hide

References

« Hide 'large scale' references
[1]"Humoral and cell-mediated autoimmunity in allergy to Aspergillus fumigatus."
Crameri R., Faith A., Hemmann S., Jaussi R., Ismail C., Menz G., Blaser K.
J. Exp. Med. 184:265-270(1996) [PubMed: 8691141] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 42202 / AF-102 / Ag 507.
[2]"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: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[3]"Comparison of the crystal structures of the human manganese superoxide dismutase and the homologous Aspergillus fumigatus allergen at 2-A resolution."
Flueckiger S., Mittl P.R.E., Scapozza L., Fijten H., Folkers G., Gruetter M.G., Blaser K., Crameri R.
J. Immunol. 168:1267-1272(2002) [PubMed: 11801664] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U53561 mRNA. Translation: AAB60779.1. Different initiation.
AAHF01000004 Genomic DNA. Translation: EAL90786.1.
RefSeqXP_752824.1. XM_747731.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKCX-ray2.00A/B/X/Y1-210[»]
ProteinModelPortalQ92450.
SMRQ92450. Positions 4-203.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ92450.

Protein family/group databases

Allergome3124. Asp f 6.0101.
76. Asp f 6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007458; CADAFUAP00007458; CADAFUAG00007458.
GeneID3509846.
GenomeReviewsGene locus sodB in contig CM000169_GR.
KEGGafm:AFUA_1G14550.

Phylogenomic databases

eggNOGfuNOG08676.
GeneTreeEFGT00050000003541.
HOGENOMHBG507761.
OMAGVDMWEH.
OrthoDBEOG42Z80G.

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]
KOK04564.
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 nameSODM_ASPFU
AccessionPrimary (citable) accession number: Q92450
Secondary accession number(s): Q4WRZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 6, 2005
Last modified: December 14, 2011
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents