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Database: UniProt/SWISS-PROT
Entry: SODM1_BACCR
LinkDB: SODM1_BACCR
Original site: SODM1_BACCR 
ID   SODM1_BACCR             Reviewed;         218 AA.
AC   Q818I1;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   07-JUN-2017, entry version 89.
DE   RecName: Full=Superoxide dismutase [Mn] 1;
DE            EC=1.15.1.1;
GN   Name=sodA1; OrderedLocusNames=BC_4272;
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
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; AAP11187.1; -; Genomic_DNA.
DR   RefSeq; NP_833986.1; NC_004722.1.
DR   RefSeq; WP_000054174.1; NC_004722.1.
DR   ProteinModelPortal; Q818I1; -.
DR   SMR; Q818I1; -.
DR   STRING; 226900.BC4272; -.
DR   PRIDE; Q818I1; -.
DR   EnsemblBacteria; AAP11187; AAP11187; BC_4272.
DR   GeneID; 1206617; -.
DR   KEGG; bce:BC4272; -.
DR   PATRIC; fig|226900.8.peg.4416; -.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
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   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   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    218       Superoxide dismutase [Mn] 1.
FT                                /FTId=PRO_0000160015.
FT   METAL        43     43       Manganese. {ECO:0000250}.
FT   METAL        98     98       Manganese. {ECO:0000250}.
FT   METAL       180    180       Manganese. {ECO:0000250}.
FT   METAL       184    184       Manganese. {ECO:0000250}.
SQ   SEQUENCE   218 AA;  24753 MW;  89865C1628247CEE CRC64;
     MSLKWQYINW EEYNNGKTRI YQIYPYAYDA LEPHFDKETM NIHHTKHHNT YITNLNAALE
     GHAELADKSV EELVANLNEV PEAIRTAVRN NGGGHANHTF FWTILSPNGG GQPVGELATA
     IEAKFGSFDA FKEEFAKAGA TRFGSGWAWL VVNNGELEVT STPNQDSPLT EGKTPVIGLD
     VWEHAYYLNY QNRRPDYIGA FWNVVDWNAA EKRYQEAK
//
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