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Database: UniProt
Entry: P53638
LinkDB: P53638
Original site: P53638 
ID   SODF_BACFR              Reviewed;         193 AA.
AC   P53638; Q64TA3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=Superoxide dismutase [Fe];
DE            EC=1.15.1.1;
GN   Name=sodB; Synonyms=sod; OrderedLocusNames=BF2527;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lai K.N., Gregory E.M.;
RL   Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nakayama K., Sasaki A.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA
RT   inversions regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD49276.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M96560; AAA22910.1; -; Genomic_DNA.
DR   EMBL; D13756; BAA02902.1; -; Genomic_DNA.
DR   EMBL; AP006841; BAD49276.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_099810.1; NC_006347.1.
DR   ProteinModelPortal; P53638; -.
DR   SMR; P53638; -.
DR   EnsemblBacteria; BAD49276; BAD49276; BF2527.
DR   GeneID; 3083785; -.
DR   KEGG; bfr:BF2527; -.
DR   PATRIC; fig|295405.11.peg.2433; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   Proteomes; UP000002197; 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    193       Superoxide dismutase [Fe].
FT                                /FTId=PRO_0000159973.
FT   METAL        27     27       Iron. {ECO:0000250}.
FT   METAL        75     75       Iron. {ECO:0000250}.
FT   METAL       159    159       Iron. {ECO:0000250}.
FT   METAL       163    163       Iron. {ECO:0000250}.
FT   CONFLICT    172    172       R -> L (in Ref. 2; BAA02902).
FT                                {ECO:0000305}.
FT   CONFLICT    176    176       H -> D (in Ref. 1; AAA22910).
FT                                {ECO:0000305}.
SQ   SEQUENCE   193 AA;  21772 MW;  3BDD25A4B3F71DC2 CRC64;
     MTYEMPKLPY ANNALEPVIS QQTIDYHYGK HLQTYVNNLN SLVPGTEYEG KTVEAIVASA
     PDGAIFNNAG QVLNHTLYFL QFAPKPAKNE PAGKLGEAIK RDFGSFENFK KEFNAASVGL
     FGSGWAWLSV DKDGKLHITK EPNGSNPVRA GLKPLLGFDV WEHAYYLDYQ NRRADHVNKL
     WEIIDWDVVE KRL
//
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