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Database: UniProt
Entry: Q92450
LinkDB: Q92450
Original site: Q92450 
ID   SODM_ASPFU              Reviewed;         210 AA.
AC   Q92450; Q4WRZ6;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 3.
DT   16-JAN-2019, entry version 140.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   AltName: Allergen=Asp f 6;
DE   Flags: Precursor;
GN   Name=sodB; ORFNames=AFUA_1G14550;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 42202 / AF-102 / Ag 507;
RX   PubMed=8691141; DOI=10.1084/jem.184.1.265;
RA   Crameri R., Faith A., Hemmann S., Jaussi R., Ismail C., Menz G.,
RA   Blaser K.;
RT   "Humoral and cell-mediated autoimmunity in allergy to Aspergillus
RT   fumigatus.";
RL   J. Exp. Med. 184:265-270(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=11801664; DOI=10.4049/jimmunol.168.3.1267;
RA   Flueckiger S., Mittl P.R.E., Scapozza L., Fijten H., Folkers G.,
RA   Gruetter M.G., Blaser K., Crameri R.;
RT   "Comparison of the crystal structures of the human manganese
RT   superoxide dismutase and the homologous Aspergillus fumigatus allergen
RT   at 2-A resolution.";
RL   J. Immunol. 168:1267-1272(2002).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mn(2+) ion per subunit.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB60779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; U53561; AAB60779.1; ALT_INIT; mRNA.
DR   EMBL; AAHF01000004; EAL90786.1; -; Genomic_DNA.
DR   RefSeq; XP_752824.1; XM_747731.1.
DR   PDB; 1KKC; X-ray; 2.00 A; A/B/X/Y=1-210.
DR   PDBsum; 1KKC; -.
DR   ProteinModelPortal; Q92450; -.
DR   SMR; Q92450; -.
DR   STRING; 5085.CADAFUBP00001380; -.
DR   Allergome; 3124; Asp f 6.0101.
DR   Allergome; 76; Asp f 6.
DR   EnsemblFungi; EAL90786; EAL90786; AFUA_1G14550.
DR   GeneID; 3509846; -.
DR   KEGG; afm:AFUA_1G14550; -.
DR   EuPathDB; FungiDB:Afu1g14550; -.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; Q92450; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   OrthoDB; 1353361at2759; -.
DR   EvolutionaryTrace; Q92450; -.
DR   Proteomes; UP000002530; Chromosome 1.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0019863; F:IgE binding; IDA:AspGD.
DR   GO; GO:0030145; F:manganese ion binding; IDA:AspGD.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0007568; P:aging; IBA:GO_Central.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allergen; Complete proteome; Manganese; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000250}.
FT   CHAIN         ?    210       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032881.
FT   METAL        29     29       Manganese.
FT   METAL        77     77       Manganese.
FT   METAL       163    163       Manganese.
FT   METAL       167    167       Manganese.
FT   CONFLICT     55     55       N -> T (in Ref. 1; AAB60779).
FT                                {ECO:0000305}.
FT   TURN         14     20       {ECO:0000244|PDB:1KKC}.
FT   HELIX        23     31       {ECO:0000244|PDB:1KKC}.
FT   HELIX        33     53       {ECO:0000244|PDB:1KKC}.
FT   HELIX        57     82       {ECO:0000244|PDB:1KKC}.
FT   HELIX        87     89       {ECO:0000244|PDB:1KKC}.
FT   HELIX        94     96       {ECO:0000244|PDB:1KKC}.
FT   HELIX        98    108       {ECO:0000244|PDB:1KKC}.
FT   HELIX       111    124       {ECO:0000244|PDB:1KKC}.
FT   STRAND      127    137       {ECO:0000244|PDB:1KKC}.
FT   STRAND      142    148       {ECO:0000244|PDB:1KKC}.
FT   STRAND      155    163       {ECO:0000244|PDB:1KKC}.
FT   HELIX       166    168       {ECO:0000244|PDB:1KKC}.
FT   HELIX       170    173       {ECO:0000244|PDB:1KKC}.
FT   HELIX       177    184       {ECO:0000244|PDB:1KKC}.
FT   HELIX       185    187       {ECO:0000244|PDB:1KKC}.
FT   HELIX       190    199       {ECO:0000244|PDB:1KKC}.
SQ   SEQUENCE   210 AA;  23390 MW;  CE701E7086E414FC CRC64;
     MSQQYTLPPL PYPYDALQPY ISQQIMELHH KKHHQTYVNG LNAALEAQKK AAEANDVPKL
     VSVQQAIKFN GGGHINHSLF WKNLAPEKSG GGKIDQAPVL KAAIEQRWGS FDKFKDAFNT
     TLLGIQGSGW GWLVTDGPKG KLDITTTHDQ DPVTGAAPVF GVDMWEHAYY LQYLNDKASY
     AKGIWNVINW AEAENRYIAG DKGGHPFMKL
//
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