ID SODC_COLGL Reviewed; 154 AA. AC O94178; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 17-JUN-2020, entry version 84. DE RecName: Full=Superoxide dismutase [Cu-Zn]; DE EC=1.15.1.1; GN Name=SOD1; OS Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum; OC Colletotrichum gloeosporioides species complex. OX NCBI_TaxID=474922; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ICMP 110146; RA Clark S.J., Templeton M.D., Sullivan P.A.; RT "A Cu-Zn superoxide dismutase from Glomerella cingulata."; RL Submitted (JUL-1998) 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. {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=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; CC Note=Binds 1 copper ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF076951; AAD19338.1; -; Genomic_DNA. DR SMR; O94178; -. DR PRIDE; O94178; -. DR GO; GO:0005737; C:cytoplasm; 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 CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1. DR Gene3D; 2.60.40.200; -; 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; PTHR10003; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR SUPFAM; SSF49329; SSF49329; 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; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..154 FT /note="Superoxide dismutase [Cu-Zn]" FT /id="PRO_0000164115" FT METAL 47 FT /note="Copper" FT /evidence="ECO:0000250" FT METAL 49 FT /note="Copper" FT /evidence="ECO:0000250" FT METAL 64 FT /note="Copper" FT /evidence="ECO:0000250" FT METAL 64 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 72 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 81 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 84 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 121 FT /note="Copper" FT /evidence="ECO:0000250" FT DISULFID 58..147 FT /evidence="ECO:0000250" SQ SEQUENCE 154 AA; 15966 MW; 177F4962166699AC CRC64; MVKAVCVVRG DSKVTGSIVF EQESESAPTK ITWDISGNDA NAKRGMHIHT FGDNTNGCTS AGPHFNPHNK THGAPEDSNR HVGDLGNIET DANGNSKGTV TDSHVKLIGP ESVIGRTIVV HGGTDDLGKG DNEESLKTGN AGPRPACGVI GISN //