SODF_HELPY
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 03-AUG-2022, entry version 123.
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; Proteobacteria; 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}.
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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.C694_01975; -.
DR PaxDb; P43312; -.
DR EnsemblBacteria; AAD07454; AAD07454; HP_0389.
DR KEGG; hpy:HP_0389; -.
DR PATRIC; fig|85962.8.peg.402; -.
DR eggNOG; COG0605; Bacteria.
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; -; 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 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
