Reviewed, UniProtKB/Swiss-Prot Q92450 (SODM_ASPFU)

Names and origin

Protein names

Recommended 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

Organism

Aspergillus fumigatus (Sartorya fumigata) [Complete proteome]

Taxonomic identifier

5085 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Disease	Allergen
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	manganese 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion By similarity

Chain

? – 210

Superoxide dismutase [Mn], mitochondrial

PRO_0000032881

Sites

Metal binding

29

1

Manganese

Metal binding

77

1

Manganese

Metal binding

163

1

Manganese

Metal binding

167

1

Manganese

Experimental info

Sequence conflict

55

1

N → T in AAB60779. Ref.1

Secondary structure

1

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210

Helix Strand Turn

Details...

Turn

14 – 20

7

Helix

23 – 31

9

Helix

33 – 53

21

Helix

57 – 82

26

Helix

87 – 89

3

Helix

94 – 96

3

Helix

98 – 108

11

Helix

111 – 124

14

Beta strand

127 – 137

11

Beta strand

142 – 148

7

Beta strand

155 – 163

9

Helix

166 – 168

3

Helix

170 – 173

4

Helix

177 – 184

8

Helix

185 – 187

3

Helix

190 – 199

10

Sequences

	Sequence		Length	Mass (Da)
	Q92450-1 [UniParc]. Last modified December 6, 2005. Version 3. Checksum: CE701E7086E414FC	FASTA	210	23,390
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
[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).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U53561 mRNA. Translation: AAB60779.1. Different initiation.
AAHF01000004 Genomic DNA. Translation: EAL90786.1.

RefSeq

XP_752824.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KKC	X-ray	2.00	A/B/X/Y	1-210	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q92450.

Genome annotation databases

GeneID

3509846.

GenomeReviews

Gene locus sodB in contig CM000169_GR.

KEGG

afm:AFUA_1G14550.

Phylogenomic databases

HOGENOM

Q92450.

OMA

PIFTADV

OrthoDB

EOG9TB5V4

Enzyme and pathway databases

BRENDA

1.15.1.1. 18841.

Family and domain databases

InterPro

IPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]

PANTHER

PTHR11404. SODismutase. 1 hit.

Pfam

PF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000349. SODismutase. 1 hit.

PRINTS

PR01703. MNSODISMTASE.

PROSITE

PS00088. SOD_MN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SODM_ASPFU

Accession

Primary (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:	November 24, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)