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Database: UniProt
Entry: Q814I6
LinkDB: Q814I6
Original site: Q814I6 
ID   SODM2_BACCR             Reviewed;         208 AA.
AC   Q814I6;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 88.
DE   RecName: Full=Superoxide dismutase [Mn] 2;
DE            EC=1.15.1.1;
GN   Name=sodA2; OrderedLocusNames=BC_5445;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 /
OS   NCIMB 9373 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC   B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(2003).
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=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AE016877; AAP12307.1; -; Genomic_DNA.
DR   RefSeq; NP_835106.1; NC_004722.1.
DR   RefSeq; WP_000094042.1; NC_004722.1.
DR   ProteinModelPortal; Q814I6; -.
DR   SMR; Q814I6; -.
DR   STRING; 226900.BC5445; -.
DR   PRIDE; Q814I6; -.
DR   EnsemblBacteria; AAP12307; AAP12307; BC_5445.
DR   GeneID; 1207785; -.
DR   KEGG; bce:BC5445; -.
DR   PATRIC; fig|226900.8.peg.5625; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; FGTGWVW; -.
DR   Proteomes; UP000001417; 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; Manganese; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    208       Superoxide dismutase [Mn] 2.
FT                                /FTId=PRO_0000160016.
FT   METAL        28     28       Manganese. {ECO:0000250}.
FT   METAL        83     83       Manganese. {ECO:0000250}.
FT   METAL       165    165       Manganese. {ECO:0000250}.
FT   METAL       169    169       Manganese. {ECO:0000250}.
SQ   SEQUENCE   208 AA;  23999 MW;  053A701A43F6FC21 CRC64;
     MSSFQLPKLS YDYDELEPHI DSNTLSIHHG KHHATYVNNL NATLENYTEL HNKSLEELLC
     NLDTLPKEIV TAVRNNGGGH YCHSLFWEVM SPRGGGEPNG DVAKVIDYYF NTFDNLKDQL
     SKAAISRFGS GYGWLVLDGE ELSVMSTPNQ DTPLQEGKIP LLVIDVWEHA YYLKYQNRRP
     EFVTNWWHTV NWDQVNEKYL QAIQSQKH
//
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