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Database: UniProt/TrEMBL
Entry: B7JMZ9_BACC0
LinkDB: B7JMZ9_BACC0
Original site: B7JMZ9_BACC0 
ID   B7JMZ9_BACC0            Unreviewed;       203 AA.
AC   B7JMZ9;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   25-OCT-2017, entry version 55.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA1 {ECO:0000313|EMBL:ACK92175.1};
GN   OrderedLocusNames=BCAH820_4295 {ECO:0000313|EMBL:ACK92175.1};
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK92175.1, ECO:0000313|Proteomes:UP000001363};
RN   [1] {ECO:0000313|EMBL:ACK92175.1, ECO:0000313|Proteomes:UP000001363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820 {ECO:0000313|EMBL:ACK92175.1,
RC   ECO:0000313|Proteomes:UP000001363};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; CP001283; ACK92175.1; -; Genomic_DNA.
DR   RefSeq; WP_001052031.1; NC_011773.1.
DR   ProteinModelPortal; B7JMZ9; -.
DR   SMR; B7JMZ9; -.
DR   EnsemblBacteria; ACK92175; ACK92175; BCAH820_4295.
DR   GeneID; 31628265; -.
DR   KEGG; bcu:BCAH820_4295; -.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   Proteomes; UP000001363; 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   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 {ECO:0000313|Proteomes:UP000001363};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ACK92175.1}.
FT   DOMAIN        3     91       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    198       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        83     83       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  22664 MW;  61B0B7D44A090D97 CRC64;
     MAKHELPNLP YAYDALEPHF DKETMNIHHT KHHNTYITNL NAALEGHAEL ADKSVEELVA
     NLNEVPEAIR TAVRNNGGGH ANHTFFWTIL SPNGGGQPVG ELATAIEAKF GSFDAFKEEF
     AKAGATRFGS GWAWLVVNNG ELEVTSTPNQ DSPLTEGKTP VIGLDVWEHA YYLNYQNRRP
     DYIGAFWNVV DWNAAEKRYQ EAK
//
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