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Database: UniProt
Entry: Q3MSU9
LinkDB: Q3MSU9
Original site: Q3MSU9 
ID   SODB_ASPNG              Reviewed;         210 AA.
AC   Q3MSU9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   05-DEC-2018, entry version 57.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sodB;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16160852; DOI=10.1007/s00438-005-0034-3;
RA   MacKenzie D.A., Guillemette T., Al-Sheikh H., Watson A.J.,
RA   Jeenes D.J., Wongwathanarat P., Dunn-Coleman N.S., van Peij N.,
RA   Archer D.B.;
RT   "UPR-independent dithiothreitol stress-induced genes in Aspergillus
RT   niger.";
RL   Mol. Genet. Genomics 274:410-418(2005).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AJ812006; CAH19233.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3MSU9; -.
DR   SMR; Q3MSU9; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000250}.
FT   CHAIN         ?    210       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000043335.
FT   METAL        29     29       Manganese. {ECO:0000250}.
FT   METAL        77     77       Manganese. {ECO:0000250}.
FT   METAL       164    164       Manganese. {ECO:0000250}.
FT   METAL       168    168       Manganese. {ECO:0000250}.
SQ   SEQUENCE   210 AA;  23693 MW;  41FA2D7450CCC1FB CRC64;
     MTSKCTLPDL PYDYDALEPI ISKQIMELHH KKHHQTYVNN LNAALASQAS ALDSNDITQL
     ISIQQKLKFN GGGHINHSLF WKNLARYDSP ATNLERSAPS LKDAIEKQWG SVKNFTDAFE
     AVLLGIQGSG WGWLVSSGKT GFLEIVTTKD QDPVTGPIPV FGVDMWEHAY YLQYLNNKAS
     YVQNIWKVIN WEEAEHRYLN GTEELGSLKL
//
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