ID A0A6J2KJL2_BOMMA Unreviewed; 154 AA. AC A0A6J2KJL2; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 19-JAN-2022, entry version 7. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393}; DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393}; GN Name=LOC114250624 {ECO:0000313|RefSeq:XP_028040379.1}; OS Bombyx mandarina (Wild silk moth) (Wild silkworm). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Bombycidae; Bombycinae; Bombyx. OX NCBI_TaxID=7092 {ECO:0000313|Proteomes:UP000504629, ECO:0000313|RefSeq:XP_028040379.1}; RN [1] {ECO:0000313|RefSeq:XP_028040379.1} RP IDENTIFICATION. RC TISSUE=Silk gland {ECO:0000313|RefSeq:XP_028040379.1}; RG RefSeq; RL Submitted (FEB-2021) to UniProtKB. CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000256|RuleBase:RU000393}. 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 Evidence={ECO:0000256|ARBA:ARBA00001605, CC ECO:0000256|RuleBase:RU000393}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000393}; CC Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU000393}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393}; CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}. 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 RefSeq; XP_028040379.1; XM_028184578.1. DR KEGG; bman:114250624; -. DR Proteomes; UP000504629; Genome assembly. 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 {ECO:0000256|ARBA:ARBA00022862}; KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000393}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000393}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000393}; KW Reference proteome {ECO:0000313|Proteomes:UP000504629}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000393}. FT DOMAIN 13..149 FT /note="Sod_Cu" FT /evidence="ECO:0000259|Pfam:PF00080" SQ SEQUENCE 154 AA; 15803 MW; B7358C67D1821563 CRC64; MPAKAVCVLR GDVSGTVFFD QQDEKSPVVV SGEVQGLTKG KHGFHVHEFG DNTNGCTSAG AHFNPEKQDH GGPSSAVRHV GDLGNIEAIE DAGVTKVSIQ DSQISLHGPN SIIGRTLVVH ADPDDLGLGG NELSKTTGNA GGRIACGVIG LAKI //