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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

sodB

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+Note: Binds 1 Mn2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Manganese
Metal bindingi77 – 771Manganese
Metal bindingi163 – 1631Manganese
Metal bindingi167 – 1671Manganese

GO - Molecular functioni

  • IgE binding Source: ASPGD
  • manganese ion binding Source: ASPGD
  • superoxide dismutase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Alternative name(s):
Allergen: Asp f 6
Gene namesi
Name:sodB
ORF Names:AFUA_1G14550
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000002530 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiFungiDB:Afu1g14550.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3124. Asp f 6.0101.
76. Asp f 6.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 210Superoxide dismutase [Mn], mitochondrialPRO_0000032881
Transit peptidei1 – ?MitochondrionBy similarity

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • IgE binding Source: ASPGD

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni14 – 207Combined sources
Helixi23 – 319Combined sources
Helixi33 – 5321Combined sources
Helixi57 – 8226Combined sources
Helixi87 – 893Combined sources
Helixi94 – 963Combined sources
Helixi98 – 10811Combined sources
Helixi111 – 12414Combined sources
Beta strandi127 – 13711Combined sources
Beta strandi142 – 1487Combined sources
Beta strandi155 – 1639Combined sources
Helixi166 – 1683Combined sources
Helixi170 – 1734Combined sources
Helixi177 – 1848Combined sources
Helixi185 – 1873Combined sources
Helixi190 – 19910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKCX-ray2.00A/B/X/Y1-210[»]
ProteinModelPortaliQ92450.
SMRiQ92450. Positions 4-203.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92450.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000013583.
InParanoidiQ92450.
KOiK04564.
OMAiQAIKFNG.
OrthoDBiEOG7W9S5R.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQQYTLPPL PYPYDALQPY ISQQIMELHH KKHHQTYVNG LNAALEAQKK
60 70 80 90 100
AAEANDVPKL VSVQQAIKFN GGGHINHSLF WKNLAPEKSG GGKIDQAPVL
110 120 130 140 150
KAAIEQRWGS FDKFKDAFNT TLLGIQGSGW GWLVTDGPKG KLDITTTHDQ
160 170 180 190 200
DPVTGAAPVF GVDMWEHAYY LQYLNDKASY AKGIWNVINW AEAENRYIAG
210
DKGGHPFMKL
Length:210
Mass (Da):23,390
Last modified:December 6, 2005 - v3
Checksum:iCE701E7086E414FC
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551N → T in AAB60779 (PubMed:8691141).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53561 mRNA. Translation: AAB60779.1. Different initiation.
AAHF01000004 Genomic DNA. Translation: EAL90786.1.
RefSeqiXP_752824.1. XM_747731.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00007458; CADAFUAP00007458; CADAFUAG00007458.
GeneIDi3509846.
KEGGiafm:AFUA_1G14550.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53561 mRNA. Translation: AAB60779.1. Different initiation.
AAHF01000004 Genomic DNA. Translation: EAL90786.1.
RefSeqiXP_752824.1. XM_747731.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KKCX-ray2.00A/B/X/Y1-210[»]
ProteinModelPortaliQ92450.
SMRiQ92450. Positions 4-203.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3124. Asp f 6.0101.
76. Asp f 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00007458; CADAFUAP00007458; CADAFUAG00007458.
GeneIDi3509846.
KEGGiafm:AFUA_1G14550.

Organism-specific databases

EuPathDBiFungiDB:Afu1g14550.

Phylogenomic databases

HOGENOMiHOG000013583.
InParanoidiQ92450.
KOiK04564.
OMAiQAIKFNG.
OrthoDBiEOG7W9S5R.

Miscellaneous databases

EvolutionaryTraceiQ92450.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiSODM_ASPFU
AccessioniPrimary (citable) accession number: Q92450
Secondary accession number(s): Q4WRZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 6, 2005
Last modified: December 9, 2015
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.