ID SODF_HELPY Reviewed; 213 AA. AC P43312; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 24-JAN-2024, entry version 130. DE RecName: Full=Superoxide dismutase [Fe]; DE EC=1.15.1.1; GN Name=sodB; OrderedLocusNames=HP_0389; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7515365; DOI=10.1016/0378-1119(94)90614-9; RA Pesci E.C., Pickett C.L.; RT "Genetic organization and enzymatic activity of a superoxide dismutase from RT the microaerophilic human pathogen, Helicobacter pylori."; RL Gene 143:111-116(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND RP CHARACTERIZATION. RC STRAIN=2012; RX PubMed=8225605; DOI=10.1128/iai.61.12.5315-5325.1993; RA Spiegelhalder C., Gerstenecker B., Kersten A., Schiltz E., Kist M.; RT "Purification of Helicobacter pylori superoxide dismutase and cloning and RT sequencing of the gene."; RL Infect. Immun. 61:5315-5325(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=151; RX PubMed=10675591; DOI=10.1111/j.1574-6968.2000.tb08965.x; RA Bereswill S., Neuner O., Strobel S., Kist M.; RT "Identification and molecular analysis of superoxide dismutase isoforms in RT Helicobacter pylori."; RL FEMS Microbiol. Lett. 183:241-245(2000). CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological systems. 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 -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000305}. 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; L24801; AAC36885.1; -; Unassigned_DNA. DR EMBL; X72618; CAA51195.1; -; Genomic_DNA. DR EMBL; AE000511; AAD07454.1; -; Genomic_DNA. DR EMBL; AJ132687; CAA10728.1; -; Genomic_DNA. DR PIR; E64568; E64568. DR RefSeq; NP_207187.1; NC_000915.1. DR PDB; 3CEI; X-ray; 2.40 A; A/B=1-212. DR PDBsum; 3CEI; -. DR AlphaFoldDB; P43312; -. DR SMR; P43312; -. DR DIP; DIP-3411N; -. DR IntAct; P43312; 4. DR MINT; P43312; -. DR STRING; 85962.HP_0389; -. DR PaxDb; 85962-C694_01975; -. DR EnsemblBacteria; AAD07454; AAD07454; HP_0389. DR KEGG; hpy:HP_0389; -. DR PATRIC; fig|85962.8.peg.402; -. DR eggNOG; COG0605; Bacteria. DR InParanoid; P43312; -. DR OrthoDB; 9803125at2; -. DR PhylomeDB; P43312; -. DR EvolutionaryTrace; P43312; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC. DR GO; GO:0071281; P:cellular response to iron ion; IDA:CollecTF. 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 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..213 FT /note="Superoxide dismutase [Fe]" FT /id="PRO_0000159985" FT BINDING 26 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 73 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 156 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT BINDING 160 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000250" FT CONFLICT 104 FT /note="K -> Q (in Ref. 3; AAD07454)" FT /evidence="ECO:0000305" FT CONFLICT 112 FT /note="S -> R (in Ref. 2; CAA51195)" FT /evidence="ECO:0000305" FT CONFLICT 124 FT /note="A -> V (in Ref. 3; AAD07454)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="A -> P (in Ref. 2; CAA51195)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="G -> E (in Ref. 3; AAD07454)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="A -> LE (in Ref. 2; CAA51195)" FT /evidence="ECO:0000305" FT TURN 15..17 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 20..26 FT /evidence="ECO:0007829|PDB:3CEI" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 30..42 FT /evidence="ECO:0007829|PDB:3CEI" FT TURN 46..49 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 52..58 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 61..78 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 89..99 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 102..115 FT /evidence="ECO:0007829|PDB:3CEI" FT STRAND 118..126 FT /evidence="ECO:0007829|PDB:3CEI" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:3CEI" FT STRAND 133..139 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 144..147 FT /evidence="ECO:0007829|PDB:3CEI" FT STRAND 150..156 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 170..179 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 183..196 FT /evidence="ECO:0007829|PDB:3CEI" FT HELIX 199..208 FT /evidence="ECO:0007829|PDB:3CEI" SQ SEQUENCE 213 AA; 24518 MW; 59ABCC4C82C2B1B2 CRC64; MFTLRELPFA KDSMGDFLSP VAFDFHHGKH HQTYVNNLNN LIKGTDFEKS SLFDILTKSS GGVFNNAAQI YNHDFYWDCL SPKATALSDE LKGALEKDFG SLEKFKEDFI KSATTLFGSG WNWAAYNLDT QKIEIIQTSN AQTPVTDKKV PLLVVDVWEH AYYIDHKNAR PVYLEKFYGH INWHFVSQCY EWAKKEGLGS VDYYINELVH KKA //