SODM_ASPFU
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 03-AUG-2022, entry version 154.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3};
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;
OC Aspergillus subgen. Fumigati.
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., 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., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., 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., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA 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 superoxide
RT dismutase and the homologous Aspergillus fumigatus allergen at 2-A
RT 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 systems.
CC {ECO:0000250|UniProtKB:P04179}.
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 Evidence={ECO:0000250|UniProtKB:P0A0J3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UQX0};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9UQX0};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P04179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9UQX0}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; Q92450; -.
DR SMR; Q92450; -.
DR STRING; 746128.CADAFUBP00001380; -.
DR Allergome; 3124; Asp f 6.0101.
DR Allergome; 76; Asp f 6.
DR PRIDE; Q92450; -.
DR EnsemblFungi; EAL90786; EAL90786; AFUA_1G14550.
DR GeneID; 3509846; -.
DR KEGG; afm:AFUA_1G14550; -.
DR VEuPathDB; FungiDB:Afu1g14550; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_2_0_1; -.
DR InParanoid; Q92450; -.
DR OMA; YEGWKGE; -.
DR OrthoDB; 1353361at2759; -.
DR EvolutionaryTrace; Q92450; -.
DR Proteomes; UP000002530; Chromosome 1.
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:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 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; Antioxidant; Manganese; Metal-binding;
KW Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..210
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032881"
FT BINDING 29
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT CONFLICT 55
FT /note="N -> T (in Ref. 1; AAB60779)"
FT /evidence="ECO:0000305"
FT TURN 14..20
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 33..53
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 57..82
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1KKC"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:1KKC"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1KKC"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1KKC"
FT HELIX 190..199
FT /evidence="ECO:0007829|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
