ID F0RN01_DEIPM Unreviewed; 209 AA. AC F0RN01; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 58. 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 OrderedLocusNames=Deipr_0987 {ECO:0000313|EMBL:ADY26143.1}; OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY26143.1, ECO:0000313|Proteomes:UP000007718}; RN [1] {ECO:0000313|Proteomes:UP000007718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM RT 20540."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADY26143.1, ECO:0000313|Proteomes:UP000007718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718}; RX PubMed=22768367; DOI=10.4056/sigs.2756060; RA Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., RA Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M., RA Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Lapidus A.; RT "Complete genome sequence of the orange-red pigmented, radioresistant RT Deinococcus proteolyticus type strain (MRP(T))."; RL Stand. Genomic Sci. 6:240-250(2012). 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|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; CP002536; ADY26143.1; -; Genomic_DNA. DR RefSeq; WP_013614752.1; NC_015161.1. DR AlphaFoldDB; F0RN01; -. DR STRING; 693977.Deipr_0987; -. DR KEGG; dpt:Deipr_0987; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_1_0; -. DR OrthoDB; 9803125at2; -. DR Proteomes; UP000007718; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1. DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, 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 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:UP000007718}. FT DOMAIN 3..89 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 98..204 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 27 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 81 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 171 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 175 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 209 AA; 23079 MW; 789886176974D3F5 CRC64; MAFELPQLPY GFDALEPHID AQTMQIHHGK HHQAYVDNAN KALEGTEWAD RDVLDVIQNL DSLPADKKGA VRNNAGGHAN HSLFWTVLSG KGGEGNQPSG ELMDAITSTF GSFDAFKEKF EDAAKTRFGS GWAWLVVKDG ALAVVSTANQ DNPLMGEAVA GTSGTPILGV DVWEHAYYLN YQNRRPDYLK AFWNVVNWDE VARRYAEAK //