ID G4NDM9_PYRO7 Unreviewed; 227 AA. AC G4NDM9; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 27-MAR-2024, entry version 55. 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=MGG_00212 {ECO:0000313|EMBL:EHA49314.1}; OS Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast OS fungus) (Magnaporthe oryzae). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia. OX NCBI_TaxID=242507 {ECO:0000313|EMBL:EHA49314.1, ECO:0000313|Proteomes:UP000009058}; RN [1] {ECO:0000313|EMBL:EHA49314.1, ECO:0000313|Proteomes:UP000009058} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958 RC {ECO:0000313|Proteomes:UP000009058}; RX PubMed=15846337; DOI=10.1038/nature03449; RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., RA Orbach M.J., Thon M., Kulkarni R., Xu J.R., Pan H., Read N.D., Lee Y.H., RA Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M., RA Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S., RA Lebrun M.H., Bohnert H., Coughlan S., Butler J., Calvo S., Ma L.J., RA Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.; RT "The genome sequence of the rice blast fungus Magnaporthe grisea."; RL Nature 434:980-986(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=70-15; RG The Broad Institute Genome Sequencing Platform; RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A., RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A., RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D., RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Magnaporthe oryzae 70-15."; RL Submitted (MAY-2011) 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. 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; CM001235; EHA49314.1; -; Genomic_DNA. DR RefSeq; XP_003718898.1; XM_003718850.1. DR AlphaFoldDB; G4NDM9; -. DR SMR; G4NDM9; -. DR STRING; 242507.G4NDM9; -. DR EnsemblFungi; MGG_00212T0; MGG_00212T0; MGG_00212. DR GeneID; 2674520; -. DR KEGG; mgr:MGG_00212; -. DR VEuPathDB; FungiDB:MGG_00212; -. DR eggNOG; KOG0876; Eukaryota. DR HOGENOM; CLU_031625_2_1_1; -. DR InParanoid; G4NDM9; -. DR OMA; DSLINWD; -. DR OrthoDB; 4839at2759; -. DR Proteomes; UP000009058; Chromosome 5. 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:UP000009058}. FT DOMAIN 36..112 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 122..223 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 59 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 104 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 190 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 194 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 227 AA; 24650 MW; CD8B8692329B0C4F CRC64; MASLIRTTPA VRGALRSRAF KPAAMASTSF VRGKATLPDL KYDYGALEPY ISAEIMELHH SKHHNTYVQG YNSAVQAIAE APTPQAAAAV APLLNFHGGG HVNHSLFWEN LAPASREGGG EPDGKLRAGI DATFGSFETF TKQMNTTLAG IQGSGWAWLA KDKTTGALSI VTRANQDPVA GNLAPLLGID AWEHAYYLQY QNRKAEYFSA IWNVINWKTV GNRFDKS //