ID SODC_ASPNC Reviewed; 154 AA. AC A2QMY6; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P00442}; DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P85978}; GN Name=sodC {ECO:0000250|UniProtKB:Q9Y8D9}; ORFNames=An07g03770; OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=425011; RN [1] {ECO:0000312|EMBL:CAK48127.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513; RX PubMed=17259976; DOI=10.1038/nbt1282; RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M., RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory Aspergillus RT niger CBS 513.88."; RL Nat. Biotechnol. 25:221-231(2007). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000250|UniProtKB:P00442}. 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:0000250|UniProtKB:P85978}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00442}; CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00442}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P00442}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00442}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00442}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00442}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000255}. 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; AM270128; CAK48127.1; -; Genomic_DNA. DR RefSeq; XP_001391459.1; XM_001391422.2. DR AlphaFoldDB; A2QMY6; -. DR SMR; A2QMY6; -. DR EnsemblFungi; CAK48127; CAK48127; An07g03770. DR GeneID; 4981643; -. DR KEGG; ang:An07g03770; -. DR VEuPathDB; FungiDB:An07g03770; -. DR HOGENOM; CLU_056632_4_1_1; -. DR OrthoDB; 3470597at2759; -. DR Proteomes; UP000006706; Chromosome 4L. DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi. DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi. DR GO; GO:1902693; C:superoxide dismutase complex; IEA:EnsemblFungi. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:EnsemblFungi. DR GO; GO:0031505; P:fungal-type cell wall organization; IEA:EnsemblFungi. DR GO; GO:0006878; P:intracellular copper ion homeostasis; IEA:EnsemblFungi. DR GO; GO:0006882; P:intracellular zinc ion homeostasis; IEA:EnsemblFungi. DR GO; GO:1901856; P:negative regulation of cellular respiration; IEA:EnsemblFungi. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi. DR GO; GO:0015680; P:protein maturation by copper ion transfer; IEA:EnsemblFungi. DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi. DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1. 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|UniProtKB:P00442" FT CHAIN 2..154 FT /note="Superoxide dismutase [Cu-Zn]" FT /evidence="ECO:0000250|UniProtKB:P00442" FT /id="PRO_0000355100" FT REGION 125..147 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 47 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 49 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 64 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 121 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P00445" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00445" FT DISULFID 58..147 FT /evidence="ECO:0000250|UniProtKB:P00442" SQ SEQUENCE 154 AA; 15960 MW; C8679562F6FB52AF CRC64; MVKAVAVIRG DSKVSGTVTF EQANENTPTT ISWNITGHDA NAERGFHVHQ FGDNTNGCTS AGPHFNPFGK THGAPEDDER HVGDLGNFKT DAEGNAVGSK QDKLVKLIGA ESVLGRTLVV HAGTDDLGRG GNEESKKTGN AGPRPACGVI GIAA //