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Database: UniProt
Entry: P35017
LinkDB: P35017
Original site: P35017 
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   05-DEC-2018, entry version 91.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae;
OC   Crotonoideae; Micrandreae; 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
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: Present in all tissues examined (leaf,
CC       petiole, root, latex, callus) with young leaves showing the
CC       highest levels in intact plants.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; L11707; AAA16792.1; -; Unassigned_DNA.
DR   PIR; S39492; S39492.
DR   ProteinModelPortal; P35017; -.
DR   SMR; P35017; -.
DR   Allergome; 380; Hev b 10.
DR   Allergome; 381; Hev b 10.0101.
DR   PRIDE; P35017; -.
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; 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   Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1     27       Mitochondrion. {ECO:0000250}.
FT   CHAIN        28    233       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032894.
FT   METAL        55     55       Manganese. {ECO:0000250}.
FT   METAL       103    103       Manganese. {ECO:0000250}.
FT   METAL       192    192       Manganese. {ECO:0000250}.
FT   METAL       196    196       Manganese. {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
//
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