SODB_ASPNG
ID SODB_ASPNG Reviewed; 210 AA.
AC Q3MSU9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1;
DE Flags: Precursor;
GN Name=sodB;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16160852; DOI=10.1007/s00438-005-0034-3;
RA MacKenzie D.A., Guillemette T., Al-Sheikh H., Watson A.J., Jeenes D.J.,
RA Wongwathanarat P., Dunn-Coleman N.S., van Peij N., Archer D.B.;
RT "UPR-independent dithiothreitol stress-induced genes in Aspergillus
RT niger.";
RL Mol. Genet. Genomics 274:410-418(2005).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AJ812006; CAH19233.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3MSU9; -.
DR SMR; Q3MSU9; -.
DR STRING; 5061.CADANGAP00001210; -.
DR VEuPathDB; FungiDB:An01g12530; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1117857; -.
DR VEuPathDB; FungiDB:ATCC64974_13320; -.
DR VEuPathDB; FungiDB:M747DRAFT_298480; -.
DR eggNOG; KOG0876; Eukaryota.
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 3: Inferred from homology;
KW Manganese; Metal-binding; Mitochondrion; Oxidoreductase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..210
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000043335"
FT BINDING 29
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23693 MW; 41FA2D7450CCC1FB CRC64;
MTSKCTLPDL PYDYDALEPI ISKQIMELHH KKHHQTYVNN LNAALASQAS ALDSNDITQL
ISIQQKLKFN GGGHINHSLF WKNLARYDSP ATNLERSAPS LKDAIEKQWG SVKNFTDAFE
AVLLGIQGSG WGWLVSSGKT GFLEIVTTKD QDPVTGPIPV FGVDMWEHAY YLQYLNNKAS
YVQNIWKVIN WEEAEHRYLN GTEELGSLKL
