ID   SODM_CHAFE              Reviewed;         224 AA.
AC   O96347;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
OS   Charybdis feriata (Crucifix crab) (Cancer feriatus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Portunidae; Charybdis.
OX   NCBI_TaxID=65693;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lin C.T., Lai Y.S., Kuo T.J., Chang T.C.;
RT   "Molecular cloning, expression, and characterization of a cDNA encoding Mn-
RT   superoxide dismutase from crab Charybdis feriatus.";
RL   Submitted (AUG-1997) 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 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.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF019411; AAD01640.1; -; mRNA.
DR   AlphaFoldDB; O96347; -.
DR   SMR; O96347; -.
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   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   Manganese; Metal-binding; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..224
FT                   /note="Superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032875"
FT   BINDING         46
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   224 AA;  24527 MW;  107CF19382E9138A CRC64;
     MLLARAFARR SLRAGLWCRQ KHTLPDLPYD YGALEPTISA EIMQLHHSKH HQTYVNNLNV
     AEEKLAEAKE KGDVSTIISL APALRFNGGG HINHSIFWQN LSADGGEPEG ELLAAINRDF
     GSVENMKNQL SAQTVAVQGS GWGWLGYIAE GALQIATCPN QDPLEATTGL VPLFGIDVWE
     HAYYLQYKNV RRIMLKPSGI SLIGRISLQG SMQQSKNATS CSGA