SODM_HEVBR
ID SODM_HEVBR Reviewed; 233 AA.
AC P35017;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=SODA;
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf;
RX PubMed=8219064; DOI=10.1007/bf00029003;
RA Miao Z., Gaynor J.J.;
RT "Molecular cloning, characterization and expression of Mn-superoxide
RT dismutase from the rubber tree (Hevea brasiliensis).";
RL Plant Mol. Biol. 23:267-277(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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Present in all tissues examined (leaf, petiole,
CC root, latex, callus) with young leaves showing the highest levels in
CC intact plants.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; L11707; AAA16792.1; -; Unassigned_DNA.
DR PIR; S39492; S39492.
DR AlphaFoldDB; P35017; -.
DR SMR; P35017; -.
DR Allergome; 380; Hev b 10.
DR Allergome; 381; Hev b 10.0101.
DR PRIDE; P35017; -.
DR OrthoDB; 1353361at2759; -.
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..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..233
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032894"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 192
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"
SQ SEQUENCE 233 AA; 25840 MW; D6C48D7A7E9A8D59 CRC64;
MALRSLVTRK NLPSAFKAAT GLGQLRGLQT FSLPDLPYDY GALEPAISGE IMQLHHQKHH
QTYITNYNKA LEQLNDAIEK GDSAAVVKLQ SAIKFNGGGH VNHSIFWKNL APVREGGGEL
PHGSLGWAID ADFGSLEKLI QLMNAEGAAL QGSGWVWLAL DKELKKLVVE TTANQDPLVT
KGPTLVPLLG IDVWEHAYYL QYKNVRPDYL KNIWKVMNWK YASEVYAKEC PSS