SODM_ONCVO
ID SODM_ONCVO Reviewed; 223 AA.
AC P41981;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sod-2;
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=7772025; DOI=10.1042/bj3080441;
RA Henkle-Duehrsen K., Tawe W., Warnecke C., Walter R.D.;
RT "Characterization of the manganese superoxide dismutase cDNA and gene from
RT the human parasite Onchocerca volvulus.";
RL Biochem. J. 308:441-446(1995).
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 -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; X82172; CAA57658.1; -; Genomic_DNA.
DR EMBL; X82171; CAA57657.1; -; mRNA.
DR PIR; S48831; S48831.
DR PIR; S55346; S48832.
DR AlphaFoldDB; P41981; -.
DR SMR; P41981; -.
DR STRING; 6282.P41981; -.
DR EnsemblMetazoa; OVOC1096a; OVOC1096a; WBGene00237905.
DR HOGENOM; CLU_031625_2_1_1; -.
DR Proteomes; UP000024404; Unassembled WGS sequence.
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;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 25..223
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032878"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT VARIANT 7
FT /note="V -> I"
SQ SEQUENCE 223 AA; 25021 MW; F6B78DAC10E02D92 CRC64;
MNLIIGVAGR LLVGKNYCLN TQRLKHVLPD LPYDYGALEP ILSAEIMQVH HGKHHAAYVN
ALNQAEEKVK EALAKGDTQA AVAGTKLMNF NTGGHINHTL FWEGLTAVKN SGEPNSELMT
AIKKDFGSLE TMIDKLNAKT IAIQGSGWGW LAYDKEMKRL QLACCPNQDL LEPTTGLIPL
FCIDVWEHAY YLQYKNLRPD FVKAIWKIAN WKIISDRYIK ARG