ID A2QIV5_ASPNC Unreviewed; 231 AA. AC A2QIV5; DT 06-MAR-2007, integrated into UniProtKB/TrEMBL. DT 06-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414}; DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414}; GN ORFNames=An04g04870 {ECO:0000313|EMBL:CAK38749.1}; 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 {ECO:0000313|EMBL:CAK38749.1, ECO:0000313|Proteomes:UP000006706}; RN [1] {ECO:0000313|EMBL:CAK38749.1, ECO:0000313|Proteomes:UP000006706} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892 RC {ECO:0000313|Proteomes:UP000006706}; 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., van den Berg M., Breestraat S., Caddick M.X., RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J., RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J., RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W., RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P., RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M., RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U., RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J., RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P., RA van Ooyen A.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:0000256|RuleBase:RU000414}. 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:RU000414}; CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}. 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; AM270077; CAK38749.1; -; Genomic_DNA. DR RefSeq; XP_001401851.1; XM_001401814.2. DR AlphaFoldDB; A2QIV5; -. DR EnsemblFungi; CAK38749; CAK38749; An04g04870. DR GeneID; 4990894; -. DR KEGG; ang:An04g04870; -. DR VEuPathDB; FungiDB:An04g04870; -. DR HOGENOM; CLU_031625_2_1_1; -. DR OrthoDB; 4839at2759; -. DR Proteomes; UP000006706; Chromosome 6L. DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi. DR GO; GO:0030145; F:manganese ion binding; IEA:EnsemblFungi. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1. DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019833; Mn/Fe_SOD_BS. DR InterPro; IPR019832; Mn/Fe_SOD_C. DR InterPro; IPR019831; Mn/Fe_SOD_N. DR InterPro; IPR036324; Mn/Fe_SOD_N_sf. DR InterPro; IPR036314; SOD_C_sf. DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1. DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1. DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 3: Inferred from homology; KW Antioxidant {ECO:0000256|ARBA:ARBA00022862}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000349-1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000414}; KW Reference proteome {ECO:0000313|Proteomes:UP000006706}. FT DOMAIN 38..117 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 127..228 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 61 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 109 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 195 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 199 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 231 AA; 25275 MW; E5E49F9CB416BF1F CRC64; MAASLVRTSA RTALRAGASA TPRTAGMAGL TFARGKATLP DLSYDYGALE PSISGKIMEL HHKNHHQTYV NSYNTAIEQL QEAQHKNDIA AQIALKPLIN FHGGGHLNHT LFWENLAPKS AGGGEPPSGA LSTAINDTFG SLEEFQNKMN AALAAIQGSG WAWLVKDKQT GHIGIKAYAN QDPVVGQFQP LLGIDAWEHA YYLQYQNRKA EYFKAIWEVI NWKAVEKRFS A //