ID   SODM_PEA                Reviewed;         233 AA.
AC   P27084; Q43069;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SODA;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=1932701; DOI=10.1007/bf00028746;
RA   Wong-Vega L., Burke J.J., Allen R.D.;
RT   "Isolation and sequence analysis of a cDNA that encodes pea manganese
RT   superoxide dismutase.";
RL   Plant Mol. Biol. 17:1271-1274(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Alaska; TISSUE=Etiolated bud;
RA   Jaradat T., Wong-Vega L., Allen R.D.;
RL   Submitted (OCT-1995) 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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; X60170; CAA42737.1; -; mRNA.
DR   EMBL; U30841; AAA74442.1; -; Genomic_DNA.
DR   PIR; S18343; DSPMN.
DR   AlphaFoldDB; P27084; -.
DR   SMR; P27084; -.
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   Manganese; Metal-binding; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           37..233
FT                   /note="Superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032901"
FT   BINDING         64
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        160
FT                   /note="Q -> QASGWV (in Ref. 1; CAA42737)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="T -> TAN (in Ref. 1; CAA42737)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="G -> W (in Ref. 1; CAA42737)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   233 AA;  25822 MW;  DB246D1FF0AF4FF9 CRC64;
     MAARTLLCRK TLSSVLRNDA KPIGAAIAAA STQSRGLHVF TLPDLAYDYG ALEPVISGEI
     MQIHHQKHHQ TYITNYNKAL EQLHDAVAKA DTSTTVKLQN AIKFNGGGHI NHSIFWKNLA
     PVSEGGGEPP KESLGWAIDT NFGSLEALIQ KINAEGAALQ WLGLDKDLKR LVVETTQDPL
     VTKGASLVPL LGIDVWEHAY YLQYKNVRPD YLKNIWKVIN WKHASEVYEK ESS