ID D5SV24_PLAL2 Unreviewed; 205 AA. AC D5SV24; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 64. 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=Plim_3497 {ECO:0000313|EMBL:ADG69310.1}; OS Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290) OS (Planctomyces limnophilus). OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Planctopirus. OX NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG69310.1, ECO:0000313|Proteomes:UP000002220}; RN [1] {ECO:0000313|EMBL:ADG69310.1, ECO:0000313|Proteomes:UP000002220} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290 RC {ECO:0000313|Proteomes:UP000002220}; RX PubMed=21304691; DOI=10.4056/sigs.1052813; RA Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S., RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S., RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of Planctomyces limnophilus type strain (Mu RT 290)."; RL Stand. Genomic Sci. 3:47-56(2010). 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; CP001744; ADG69310.1; -; Genomic_DNA. DR RefSeq; WP_013111741.1; NC_014148.1. DR AlphaFoldDB; D5SV24; -. DR STRING; 521674.Plim_3497; -. DR KEGG; plm:Plim_3497; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_1_0; -. DR OrthoDB; 9803125at2; -. DR Proteomes; UP000002220; 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:UP000002220}. FT DOMAIN 3..89 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 97..198 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 82 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 169 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 205 AA; 22355 MW; 79A06F950339539E CRC64; MPFTLPALPY APAALEPHID AQTMEIHHGK HHQAYINNAN KALEGHPELA ALTAEQLISD LSKVPEGIRT VIRNNAGGHA NHSLFWTVLA PSAGGTPTGA LEAAINHTFG TFDAFKEKFN AAATTRFGSG WAWLSVDSKG GLVVESTPNQ DSPLMEGRTP ILGLDVWEHA YYLKYQNRRP DYIASFWNIV NWPEVSKRFA AAGGK //