ID Q7VF46_HELHP Unreviewed; 211 AA. AC Q7VF46; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 107. 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=sodF {ECO:0000313|EMBL:AAP78429.1}; GN OrderedLocusNames=HH_1832 {ECO:0000313|EMBL:AAP78429.1}; OS Helicobacter hepaticus (strain ATCC 51449 / 3B1). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=235279 {ECO:0000313|EMBL:AAP78429.1, ECO:0000313|Proteomes:UP000002495}; RN [1] {ECO:0000313|EMBL:AAP78429.1, ECO:0000313|Proteomes:UP000002495} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51449 / 3B1 {ECO:0000313|Proteomes:UP000002495}; RX PubMed=12810954; DOI=10.1073/pnas.1332093100; RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B., RA Shen Z., Weber J., Frosch M., Fox J.G.; RT "The complete genome sequence of the carcinogenic bacterium Helicobacter RT hepaticus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(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 -!- 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 --------------------------------------------------------------------------- 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; AE017125; AAP78429.1; -; Genomic_DNA. DR RefSeq; WP_011116671.1; NC_004917.1. DR AlphaFoldDB; Q7VF46; -. DR STRING; 235279.HH_1832; -. DR GeneID; 82136339; -. DR KEGG; hhe:HH_1832; -. DR eggNOG; COG0605; Bacteria. DR HOGENOM; CLU_031625_0_0_7; -. DR OrthoDB; 9803125at2; -. DR Proteomes; UP000002495; 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:UP000002495}. FT DOMAIN 2..81 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 89..188 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 26 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 73 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 156 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 160 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 211 AA; 24284 MW; 2281DB287F1AF50C CRC64; MFELRKLPYG KNEFNGFISE QTFEYHYGKH HQTYVNNLNN LIKGTEFENA ELGDIILKSS GGIFNNAAQV YNHDFYWDCL SPKESALSAE LSAAINAEFG SLDVFKEKFL ASSTTLFGSG WNWLVYNTQS KKLEIVQTSN AATPATDSKV PLLVVDVWEH AYYIDHRNAR PAYLEAFWKH INWAFVSRAY EWALKEGLQS FKFYINGIHK K //