ID Q7NV42_CHRVO Unreviewed; 192 AA. AC Q7NV42; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 116. 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 Name=sodB1 {ECO:0000313|EMBL:AAQ60175.1}; GN OrderedLocusNames=CV_2504 {ECO:0000313|EMBL:AAQ60175.1}; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC OS 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ60175.1, ECO:0000313|Proteomes:UP000001424}; RN [1] {ECO:0000313|EMBL:AAQ60175.1, ECO:0000313|Proteomes:UP000001424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757 {ECO:0000313|Proteomes:UP000001424}; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P., RA de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J., RA de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M., RA Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S., RA Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., RA Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., RA Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N., RA Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., RA Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., RA Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M., RA Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A., RA Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P., RA Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., RA Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F., RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., RA Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C., RA Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M., RA Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C., RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). 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; AE016825; AAQ60175.1; -; Genomic_DNA. DR RefSeq; WP_011136051.1; NC_005085.1. DR AlphaFoldDB; Q7NV42; -. DR STRING; 243365.CV_2504; -. DR GeneID; 66368254; -. DR KEGG; cvi:CV_2504; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_0_4; -. DR OrthoDB; 9803125at2; -. DR Proteomes; UP000001424; 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; PTHR42769; SUPEROXIDE DISMUTASE; 1. DR PANTHER; PTHR42769:SF3; SUPEROXIDE DISMUTASE [FE] 2, CHLOROPLASTIC; 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:UP000001424}. FT DOMAIN 2..81 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 89..190 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 74 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 157 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 161 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 192 AA; 21590 MW; 5F70C6A786C612A0 CRC64; MEHKLPELPY ALDALAPHIS KETLEFHYGK HHQTYITNLN NLIKGTEFEN ASLEEIVKKS SGGIFNNAAQ VWNHTFYWFG LAPNAGGQPT GALADAINAK WGSFDEFKKA FTQTAIGTFG SGWAWLVKNS DGSLDLVSTS NAATPLTTDK KPLLTCDVWE HAYYIDYRNS RPNYLEHFWA LVNWDFVAKN FA //