ID Q7NZQ4_CHRVO Unreviewed; 234 AA. AC Q7NZQ4; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 117. 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=sodB2 {ECO:0000313|EMBL:AAQ58542.1}; GN OrderedLocusNames=CV_0867 {ECO:0000313|EMBL:AAQ58542.1}; 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:AAQ58542.1, ECO:0000313|Proteomes:UP000001424}; RN [1] {ECO:0000313|EMBL:AAQ58542.1, 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; AAQ58542.1; -; Genomic_DNA. DR AlphaFoldDB; Q7NZQ4; -. DR STRING; 243365.CV_0867; -. DR KEGG; cvi:CV_0867; -. 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 InterPro; IPR006311; TAT_signal. 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. DR PROSITE; PS51318; TAT; 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}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..35 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 36..234 FT /note="Superoxide dismutase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004289281" FT DOMAIN 41..122 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 132..230 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 63 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 115 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 197 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 201 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 234 AA; 25525 MW; 12CBB71B08E017C9 CRC64; MPDPNAELSR RGFLLSAAGS LAALALPGLP GAAHASSAQV LPPLPYADNA LEPVISARTI GFHYGKHHKA YLDNLNKLIA GRDYADLPLE DILTRSFGPA SDAAVFNNAA QLWNHTFYWR SMRPKGGGIP PQGLREKIEA SFGSVDACKR QLAGAAISQF GSGWAWLVQD GDKLRVVKTG NADNPLTSGL TPLLNVDVWE HAYYLDYQNR RADYVNAVLD KLIDWEFAQR NLKA //