ID Q7WYN0_AERSS Unreviewed; 194 AA. AC Q7WYN0; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414}; DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414}; GN Name=sodB {ECO:0000313|EMBL:AAP85514.1}; GN ORFNames=ASJ32_14395 {ECO:0000313|EMBL:PJZ14413.1}, AXA69_000995 GN {ECO:0000313|EMBL:QHU94445.1}; OS Aeromonas salmonicida subsp. salmonicida. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=29491 {ECO:0000313|EMBL:AAP85514.1}; RN [1] {ECO:0000313|EMBL:AAP85514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A449 {ECO:0000313|EMBL:AAP85514.1}; RX PubMed=12867441; DOI=10.1128/JB.185.15.4336-4344.2003; RA Dacanay A., Johnson S.C., Bjornsdottir R., Ebanks R.O., Ross N.W., RA Reith M., Singh R.K., Hiu J., Brown L.L.; RT "Molecular characterization and quantitative analysis of superoxide RT dismutases in virulent and avirulent strains of Aeromonas salmonicida RT subsp. salmonicida."; RL J. Bacteriol. 185:4336-4344(2003). RN [2] {ECO:0000313|EMBL:AAP85514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A449 {ECO:0000313|EMBL:AAP85514.1}; RA Singh R.K., Curtis B., Kozera C., Reith M., Han Y., Boyd J.M., Stone C., RA Welsh J., Munholland J., Murphy C., Dacanay A., Douglas S., Ebanks R.O., RA Ewart V.K., Johnson S.C., Ross N.W., Sensen C., Tsoi S., Brown L.L.; RT "The Genome Sequence of Aeromonas salmonicida subsp. salmonicida strain RT A449."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:PJZ14413.1, ECO:0000313|Proteomes:UP000232113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M22710-11 {ECO:0000313|EMBL:PJZ14413.1, RC ECO:0000313|Proteomes:UP000232113}; RA Vincent A.T., Emond-Rheault J.-G., Charette S.J.; RT "Draft genome sequence of Aeromonas salmonicida subsp. salmonicida reveals RT a plasticity of AsaGEI2a."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:QHU94445.1, ECO:0000313|Proteomes:UP000077360} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J223 {ECO:0000313|EMBL:QHU94445.1, RC ECO:0000313|Proteomes:UP000077360}; RA Santander J., Valderrama K., Vasquez I., Segovia C., Hossain A., RA Cipriano R., Gnanagobal H.; RT "Aeromonas salmonicida J223 completed genome."; RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases. 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; AY321353; AAP85514.1; -; Genomic_DNA. DR EMBL; LMTT01000030; PJZ14413.1; -; Genomic_DNA. DR EMBL; CP048223; QHU94445.1; -; Genomic_DNA. DR RefSeq; WP_005319233.1; NZ_MIIU01000043.1. DR AlphaFoldDB; Q7WYN0; -. DR GeneID; 79879028; -. DR PATRIC; fig|29491.14.peg.1575; -. DR OMA; DSLINWD; -. DR Proteomes; UP000077360; Chromosome. DR Proteomes; UP000232113; Unassembled WGS sequence. 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}. FT DOMAIN 3..82 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 89..191 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 158 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 162 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 194 AA; 21584 MW; 1D59B7F4AF063B3B CRC64; MAFELPALPY AINALEPHIS QETLEYHHGK HHNTYVVNLN NLVPGTEFEG KSLEEIIKTS TGGIFNNAAQ IWNHTFYWHC LSPNGGNEPT GALADAINKA FGSFAEFKDA FTKSAIGNFG SSWTWLVKKA DGSLAIVNTS NAGCPLTEAG TTPLLTVDLW EHAYYIDFRN LRPKYMETFW TLVNWEFVAK NLAA //