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 24-JAN-2024, entry version 120.
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; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; 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 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 family.
CC {ECO:0000305}.
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DR EMBL; L19462; AAA72021.2; -; mRNA.
DR PIR; A48684; A48684.
DR AlphaFoldDB; P41979; -.
DR SMR; P41979; -.
DR STRING; 4577.P41979; -.
DR MaizeGDB; 47587; -.
DR InParanoid; P41979; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P41979; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0030145; F:manganese 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; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 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 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..233
FT /note="Superoxide dismutase [Mn] 3.3, mitochondrial"
FT /id="PRO_0000032897"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 105
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"
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
//
