ID   SODM_PRUPE              Reviewed;         228 AA.
AC   Q9SM64;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SOD; Synonyms=MNSOD1;
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000312|EMBL:CAB56851.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Chiripa {ECO:0000269|PubMed:12073034};
RC   TISSUE=Leaf {ECO:0000312|EMBL:CAB56851.1};
RX   PubMed=12073034; DOI=10.1007/s00438-002-0664-7;
RA   Bagnoli F., Giannino D., Caparrini S., Camussi A., Mariotti D.,
RA   Racchi M.L.;
RT   "Molecular cloning, characterisation and expression of a manganese
RT   superoxide dismutase gene from peach (Prunus persica L. Batsch).";
RL   Mol. Genet. Genomics 267:321-328(2002).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000250}.
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:0000255|RuleBase:RU000414, ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q92450};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q92450};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11796}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed most abundantly in parts of the plant
CC       which exhibit a high metabolic activity. Expressed in pre-shooting
CC       flower buds, vegetative buds, immature fruits and fully expanded leaves
CC       of basal shoots and seedlings. {ECO:0000269|PubMed:12073034}.
CC   -!- DEVELOPMENTAL STAGE: The level of expression in seedlings and in
CC       juvenile plants is higher than the level of expression in adult plants.
CC       {ECO:0000269|PubMed:12073034}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000255|RuleBase:RU000414, ECO:0000305}.
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DR   EMBL; AJ238316; CAB56851.1; -; mRNA.
DR   PIR; T50828; T50828.
DR   AlphaFoldDB; Q9SM64; -.
DR   SMR; Q9SM64; -.
DR   PRIDE; Q9SM64; -.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; NAS:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; NAS:UniProtKB.
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   Manganese; Metal-binding; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..228
FT                   /note="Superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032902"
FT   BINDING         52
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   228 AA;  25455 MW;  A32DA57F552F18AB CRC64;
     MALRTLVSRR TLATGLGFRQ QLRGLQTFSL PDLPYNYGAL EPAISGDIMQ LHHQNHHQTY
     VTNYNKALEQ LHDAISKGDA PTVAKLHSAI KFNGGGHINH SIFWKNLAPV REGGGEPPKG
     SLGWAIDTNF GSLEALVQKM NAEGAALQGS GWVWLALDKE LKKLVVETTA NQDPLVTKGP
     TLVPLLGIDV WEHAYYLQYK NVRPDYLKNI WKVINWKYAS EVYEKESP