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Database: UniProt
Entry: P41979
LinkDB: P41979
Original site: P41979 
ID   SODM3_MAIZE             Reviewed;         233 AA.
AC   P41979;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   13-FEB-2019, entry version 104.
DE   RecName: Full=Superoxide dismutase [Mn] 3.3, mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SODA.2; Synonyms=SOD3.3;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
OC   Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8415698; DOI=10.1073/pnas.90.20.9310;
RA   Zhu D., Scandalios J.G.;
RT   "Maize mitochondrial manganese superoxide dismutases are encoded by a
RT   differentially expressed multigene family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9310-9314(1993).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       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   -!- TISSUE SPECIFICITY: Predominantly expressed in the embryo late in
CC       embryogenesis.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; L19462; AAA72021.2; -; mRNA.
DR   PIR; A48684; A48684.
DR   UniGene; Zm.73549; -.
DR   ProteinModelPortal; P41979; -.
DR   SMR; P41979; -.
DR   PRIDE; P41979; -.
DR   MaizeGDB; 47587; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:AgBase.
DR   GO; GO:0006970; P:response to osmotic stress; IEP:AgBase.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Complete proteome; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1     29       Mitochondrion. {ECO:0000250}.
FT   CHAIN        30    233       Superoxide dismutase [Mn] 3.3,
FT                                mitochondrial.
FT                                /FTId=PRO_0000032897.
FT   METAL        57     57       Manganese. {ECO:0000250}.
FT   METAL       105    105       Manganese. {ECO:0000250}.
FT   METAL       194    194       Manganese. {ECO:0000250}.
FT   METAL       198    198       Manganese. {ECO:0000250}.
SQ   SEQUENCE   233 AA;  25448 MW;  061160B89B195A96 CRC64;
     MALRTLASKN ALSFALGGAA RPSAESARGV TTVALPDLSY DFGALEPVIS GEIMRLHHQK
     NHATYVVNYN KALEQIDDVV VKGDDSAVVQ LQGAIKFNGG GHVNHSIFWK NLKPISEGGG
     EPPHGKLGWA IDEDFGSFEA LVKRMNAEGA ALQGSGWVWL ALDKEAKKVS VETTANQDPL
     VTKGASLVPL LGIDVWEHAY YLQYKNVRPD YLNNIWKVMN WKYAGEVYEN VLA
//
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