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SODM_GANMI
ID   SODM_GANMI              Reviewed;         200 AA.
AC   Q92429;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3};
DE   AltName: Full=Mn-SOD;
DE   Flags: Precursor;
OS   Ganoderma microsporum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=34462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RSH 0821;
RA   Wang H.-F.;
RT   "Studies of manganese-superoxide dismutase gene of Ganoderma.";
RL   Thesis (1996), National Taiwan University, Taiwan.
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   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; U56403; AAB07360.1; -; mRNA.
DR   EMBL; U56127; AAB16782.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q92429; -.
DR   SMR; Q92429; -.
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; 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   2: Evidence at transcript level;
KW   Antioxidant; Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..200
FT                   /note="Superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032883"
FT   BINDING         27
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         72
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         165
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
SQ   SEQUENCE   200 AA;  22170 MW;  E39DFC7E1708961F CRC64;
     MAHVLPDLPY AYNALEPFIS QQIMELHHKK HHQTYVNSLN AAEQAYAKAS TPKERIALQS
     ALKFNGGGHI NHSLFWKNLA PAKSEGKGNG GALADGPLKS AIEQNWGSVD NFIKEFNATT
     AAIQGSGWGW LGLNPATKRL EITTTANQDP LLSHVPIIGV DIWEHAFYLQ YLNVKADYLA
     AIWIVINFKE AERRLIEATK
 
 
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