ID   SODM1_MAIZE             Reviewed;         235 AA.
AC   P09233;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   04-NOV-2026, entry version 153.
DE   RecName: Full=Superoxide dismutase [Mn] 3.1, mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SODA.4; Synonyms=SOD3, SOD3.1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 64A;
RX   PubMed=2461225; DOI=10.1016/0167-4781(88)90025-5;
RA   Redinbaugh M.G., Wadsworth G.T., Scandalios J.G.;
RT   "Isolation and characterization of a cDNA for mitochondrial manganese
RT   superoxide dismutase (SOD-3) of maize and its relation to other manganese
RT   superoxide dismutases.";
RL   Biochim. Biophys. Acta 951:61-70(1988).
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 superoxide + 2 H(+) = 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; X12540; CAA31058.1; -; mRNA.
DR   RefSeq; NP_001105742.2; NM_001112272.3.
DR   AlphaFoldDB; P09233; -.
DR   SMR; P09233; -.
DR   FunCoup; P09233; 2657.
DR   STRING; 4577.P09233; -.
DR   PaxDb; 4577-P09233; -.
DR   GeneID; 542764; -.
DR   KEGG; zma:542764; -.
DR   MaizeGDB; 47587; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   InParanoid; P09233; -.
DR   OMA; AACSQHC; -.
DR   OrthoDB; 239262at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:AgBase.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:AgBase.
DR   GO; GO:0009635; P:response to herbicide; IDA:AgBase.
DR   GO; GO:0006979; P:response to oxidative stress; TAS:AgBase.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEP:AgBase.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:AgBase.
DR   FunFam; 1.10.287.990:FF:000001; Superoxide dismutase; 1.
DR   FunFam; 3.55.40.20:FF:000002; Superoxide dismutase; 1.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR050265; Fe/Mn_Superoxide_Dismutase.
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   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   2: Evidence at transcript level;
KW   Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..235
FT                   /note="Superoxide dismutase [Mn] 3.1, mitochondrial"
FT                   /id="PRO_0000032895"
FT   BINDING         59
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   235 AA;  25545 MW;  AD51BAD0F44FDE56 CRC64;
     MALRTLASKK VLSFPFGGAG RPLAAAASAR GVTTVTLPDL SYDFGALEPA ISGEIMRLHH
     QKHHATYVAN YNKALEQLET AVSKGDASAV VQLQAAIKFN GGGHVNHSIF WKNLKPISEG
     GGEPPHGKLG WAIDEDFGSF EALVKKMNAE GAALQGSGWV WLALDKEAKK VSVETTANQD
     PLVTKGASLV PLLGIDVWEH AYYLQYKNVR PDYLNNIWKV MNWKYAGEVY ENVLA
//