ID   SODC_DROMA              Reviewed;         153 AA.
AC   P61853; P00444; Q9VTF6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P61851};
DE            EC=1.15.1.1;
DE   AltName: Full=Superoxide dismutase 1 {ECO:0000250|UniProtKB:P61851};
GN   Name=Sod1 {ECO:0000250|UniProtKB:P61851};
GN   Synonyms=Sod {ECO:0000250|UniProtKB:P61851};
OS   Drosophila mauritiana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Arxontaki K., Kastanis P., Tsakas S., Loukas M., Eliopoulos E.;
RT   "Phylogenetic analysis of Drosophila melanogaster group based on Cu-Zn
RT   superoxide dismutase gene sequences.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000250|UniProtKB:P61851}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 superoxide + 2 H(+) = 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         Evidence={ECO:0000250|UniProtKB:P61851};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00441};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00441};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00441};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00441};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00441}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; AF127158; AAF23597.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61853; -.
DR   SMR; P61853; -.
DR   EnsemblMetazoa; XM_033303047.1; XP_033158938.1; LOC117140245.
DR   Proteomes; UP000515162; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   FunFam; 2.60.40.200:FF:000001; Superoxide dismutase [Cu-Zn]; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..153
FT                   /note="Superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000164086"
FT   BINDING         45
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         47
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         62
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   BINDING         119
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
FT   DISULFID        56..145
FT                   /evidence="ECO:0000250|UniProtKB:P00441"
SQ   SEQUENCE   153 AA;  15699 MW;  4A6AAAA1EB545E70 CRC64;
     MVVKAVCVIN GDAKGTVFFE QESSGTPVKV SGEVCGLAKG LHGFHVHEFG DNTNGCMSSG
     PHFNPYGKEH GAPVDENRHL GDLGNIEATG DCPTKVNITD SKITLFGADS IIGRTVVVHA
     DADDLGQGGH ELSKSTGNAG ARIGCGVIGI AKV
//