ID J0DWH8_HELPX Unreviewed; 213 AA. AC J0DWH8; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 29-SEP-2021, entry version 26. 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:EJB90433.1}; GN ORFNames=HPHPH19_0768 {ECO:0000313|EMBL:EJB90433.1}; OS Helicobacter pylori Hp H-19. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=992066 {ECO:0000313|EMBL:EJB90433.1, ECO:0000313|Proteomes:UP000005191}; RN [1] {ECO:0000313|EMBL:EJB90433.1, ECO:0000313|Proteomes:UP000005191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hp H-19 {ECO:0000313|EMBL:EJB90433.1, RC ECO:0000313|Proteomes:UP000005191}; RX PubMed=23661595; DOI=10.1111/2049-632X.12045; RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M., RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K., RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.; RT "Genome sequences of 65 Helicobacter pylori strains isolated from RT asymptomatic individuals and patients with gastric cancer, peptic ulcer RT disease, or gastritis."; RL Pathog. Dis. 68:39-43(2013). 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 -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000256|ARBA:ARBA00001962}; CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EJB90433.1}. 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; AKPE01000003; EJB90433.1; -; Genomic_DNA. DR RefSeq; WP_000494622.1; NZ_AKPE01000003.1. DR EnsemblBacteria; EJB90433; EJB90433; HPHPH19_0768. DR PATRIC; fig|992066.3.peg.743; -. DR Proteomes; UP000005191; 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; -; 1. DR Gene3D; 3.55.40.20; -; 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 Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF46609; SSF46609; 1. DR SUPFAM; SSF54719; SSF54719; 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 2..81 FT /note="Sod_Fe_N" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 89..188 FT /note="Sod_Fe_C" FT /evidence="ECO:0000259|Pfam:PF02777" FT METAL 26 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT METAL 73 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT METAL 156 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT METAL 160 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 213 AA; 24532 MW; 7835C2FAC7A5B6C0 CRC64; MFTLRELPFA KDSMGDFLSP VAFDFHHGKH HQTYVNNLNN LIKGTDFEKS SLFAILTKSS GGVFNNAAQI YNHDFYWDCL SPKATALSDE LKGALEKDFG SLEKFKEDFI KSATTLFGSG WNWAAYNLDT QKIEIIQTSN AQTPVTDKKV PLLVVDVWEH AYYIDHKNAR PVYLEKFYEH VNWHFVSQCY EWAKKEGLGS VDYYINELVH KKA //