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
