ID A5FGP6_FLAJ1 Unreviewed; 260 AA. AC A5FGP6; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 91. 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=Fjoh_2595 {ECO:0000313|EMBL:ABQ05622.1}; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05622.1, ECO:0000313|Proteomes:UP000006694}; RN [1] {ECO:0000313|EMBL:ABQ05622.1, ECO:0000313|Proteomes:UP000006694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / RC UW101 {ECO:0000313|Proteomes:UP000006694}; RX PubMed=19717629; DOI=10.1128/AEM.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., RA Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). 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; CP000685; ABQ05622.1; -; Genomic_DNA. DR RefSeq; WP_012024661.1; NZ_MUGZ01000009.1. DR AlphaFoldDB; A5FGP6; -. DR STRING; 376686.Fjoh_2595; -. DR KEGG; fjo:Fjoh_2595; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_1_10; -. DR OrthoDB; 9803125at2; -. DR Proteomes; UP000006694; 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 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; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000414}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000414}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..260 FT /note="Superoxide dismutase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030164433" FT DOMAIN 55..137 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 145..248 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" SQ SEQUENCE 260 AA; 29870 MW; 5DAE11F915DAC2D1 CRC64; MKKIIVLFSI LPSFILLFSC NDNNKLTEVV EVPLPTKEEK IVIGSPNDVK ADPGSFELTK LPFAYDGLSP ALRSLTMETH YSKHYLSYTN NFNKAIVSTE FENMPIEDIL KKLDLNNAKL RQNAGGYYNH TLYFNILTPK EQTPKDTLSG SINKEFGSFN NLTTQFKGQA EKQFGSGWVW LVVDRYGKLQ ITTTEDQDNP LMKNALIPGT PILGIDLWEH AYYLDYQNRK GSYIDAFYEH INWEKVNEYY IEALKKVKKV //