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Database: UniProt
Entry: Q9P4T6
LinkDB: Q9P4T6
Original site: Q9P4T6 
ID   SODM_AGABI              Reviewed;         200 AA.
AC   Q9P4T6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   05-DEC-2018, entry version 75.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sod;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Horst U3;
RA   Eastwood D.C., Bains N.K., Henderson J., Burton K.S.;
RT   "Oxidative stress in the harvested mushroom, Agaricus bisporus.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AJ404469; CAB94731.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9P4T6; -.
DR   SMR; Q9P4T6; -.
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; 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:0000255}.
FT   CHAIN         ?    200       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032880.
FT   METAL        27     27       Manganese. {ECO:0000250}.
FT   METAL        72     72       Manganese. {ECO:0000250}.
FT   METAL       157    157       Manganese. {ECO:0000250}.
FT   METAL       161    161       Manganese. {ECO:0000250}.
SQ   SEQUENCE   200 AA;  22194 MW;  9758B1DD1F674F19 CRC64;
     MAHVLPDLPY AYDALEPYIS RQIMELHHKK TSSDLCECAQ HCRGCLRHST AVVGGFDLSL
     FFILTTLGHI NHSLFWQNLA PAAGAGGQLK PGPLKDAIDQ TFGGLDNLKK EFNTTTAGIQ
     GSGWGWLGVN PSNKRLEIST TPNQDPLLNL VPIIGVDIWE HAFYLQYLNV KADYLNAIWS
     VINFDEAQRR YVEATQGSKL
//
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