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Database: UniProt
Entry: O75007
LinkDB: O75007
Original site: O75007 
ID   SODM_PENCH              Reviewed;         210 AA.
AC   O75007;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   05-DEC-2018, entry version 92.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SOD;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PROTEIN SEQUENCE OF
RP   84-102; 118-135 AND 181-190.
RC   STRAIN=AS-P-78;
RX   PubMed=9644201; DOI=10.1007/s002940050351;
RA   Diez B., Schleissner C., Moreno M.A., Rodriguez M., Collados A.,
RA   Barredo J.L.;
RT   "The manganese superoxide dismutase from the penicillin producer
RT   Penicillium chrysogenum.";
RL   Curr. Genet. 33:387-394(1998).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF026790; AAC36585.1; -; Genomic_DNA.
DR   EMBL; AF026523; AAC36583.1; -; mRNA.
DR   ProteinModelPortal; O75007; -.
DR   SMR; O75007; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   PhylomeDB; O75007; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    210       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032886.
FT   METAL        30     30       Manganese. {ECO:0000250}.
FT   METAL        78     78       Manganese. {ECO:0000250}.
FT   METAL       166    166       Manganese. {ECO:0000250}.
FT   METAL       170    170       Manganese. {ECO:0000250}.
SQ   SEQUENCE   210 AA;  23128 MW;  E8A850D50F0A7B99 CRC64;
     MTSQTHTLPP LPYAYDALEP VISKQIMELH HQKHHQTYIN NLNAALSAQA SATASNDVPT
     LISLQQKLRF NGGGHINHSL FWKNLTPPGT PANDIAGAPA LREAIVSRWG SHEAFVKAFG
     AELLGLQGSG WGWLVSKGGA KGRLEIVTTK DQDPVNAPDV PVFGVDMWEH AYYLQYLNNK
     AGYVEGIWKI IHWAEAEKRY TAGVENPLKL
//
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