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 03-NOV-2009, entry version 46. DE RecName: Full=Superoxide dismutase [Cu-Zn]; DE EC=1.15.1.1; GN Name=SOD1; OS Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella OS cingulata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreomycetidae incertae sedis; OC Glomerellaceae; Glomerella. 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 (By similarity). CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion per subunit (By similarity). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. 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 HSSP; P00441; 1OZU. DR BRENDA; 1.15.1.1; 39832. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro. DR InterPro; IPR018152; SOD_Cu/Zn_BS. DR InterPro; IPR001424; SOD_Cu_Zn. DR Gene3D; G3DSA:2.60.40.200; SOD_Cu_Zn; 1. DR PANTHER; PTHR10003; SOD_Cu_Zn; 1. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 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 1 Removed (By similarity). FT CHAIN 2 154 Superoxide dismutase [Cu-Zn]. FT /FTId=PRO_0000164115. FT METAL 47 47 Copper (By similarity). FT METAL 49 49 Copper (By similarity). FT METAL 64 64 Copper (By similarity). FT METAL 64 64 Zinc (By similarity). FT METAL 72 72 Zinc (By similarity). FT METAL 81 81 Zinc (By similarity). FT METAL 84 84 Zinc (By similarity). FT METAL 121 121 Copper (By similarity). FT DISULFID 58 147 By similarity. SQ SEQUENCE 154 AA; 15966 MW; 177F4962166699AC CRC64; MVKAVCVVRG DSKVTGSIVF EQESESAPTK ITWDISGNDA NAKRGMHIHT FGDNTNGCTS AGPHFNPHNK THGAPEDSNR HVGDLGNIET DANGNSKGTV TDSHVKLIGP ESVIGRTIVV HGGTDDLGKG DNEESLKTGN AGPRPACGVI GISN //