SODF_BACFR
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 03-AUG-2022, entry version 112.
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 inversions
RT 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 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 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD49276.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 AlphaFoldDB; P53638; -.
DR SMR; P53638; -.
DR STRING; 295405.BF2527; -.
DR EnsemblBacteria; BAD49276; BAD49276; BF2527.
DR KEGG; bfr:BF2527; -.
DR PATRIC; fig|295405.11.peg.2433; -.
DR HOGENOM; CLU_031625_0_0_10; -.
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; 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 3: Inferred from homology;
KW Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..193
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000159973"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 172
FT /note="R -> L (in Ref. 2; BAA02902)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="H -> D (in Ref. 1; AAA22910)"
FT /evidence="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