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Database: UniProt
Entry: Q9ZKE6
LinkDB: Q9ZKE6
Original site: Q9ZKE6 
ID   SODF_HELPJ              Reviewed;         213 AA.
AC   Q9ZKE6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JAN-2019, entry version 111.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; Synonyms=sodF; OrderedLocusNames=jhp_0992;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori
OS   J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
RA   Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
RA   Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
RA   Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human
RT   gastric pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AE001439; AAD06571.1; -; Genomic_DNA.
DR   PIR; E71861; E71861.
DR   RefSeq; WP_000494616.1; NZ_CP011330.1.
DR   ProteinModelPortal; Q9ZKE6; -.
DR   SMR; Q9ZKE6; -.
DR   STRING; 85963.jhp0992; -.
DR   EnsemblBacteria; AAD06571; AAD06571; jhp_0992.
DR   KEGG; hpj:jhp_0992; -.
DR   PATRIC; fig|85963.30.peg.1599; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; HPYL85963:G1G1A-1059-MONOMER; -.
DR   Proteomes; UP000000804; 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; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   Complete proteome; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN         1    213       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159986.
FT   METAL        26     26       Iron. {ECO:0000250}.
FT   METAL        73     73       Iron. {ECO:0000250}.
FT   METAL       156    156       Iron. {ECO:0000250}.
FT   METAL       160    160       Iron. {ECO:0000250}.
SQ   SEQUENCE   213 AA;  24532 MW;  7955C3ACF2C5B4C0 CRC64;
     MFTLRELPFA KDSMGDFLSP VAFDFHHGKH HQTYVNNLNN LIKGTDFEKS SLFAILTKSS
     GGVFNNAAQI YNHDFYWDCL SPKATALSDE LKEALEKDFG SLEKFKEDFI KSATTLFGSG
     WNWAAYNLDT QKIEIIQTSN AQTPVTDKKV PLLVVDVWEH AYYIDHKNAR PVYLEKFYGH
     VNWHFVSQCY EWAKKEGLGS VDYYINELVH KKA
//
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