ID   A7GN06_BACCN            Unreviewed;       304 AA.
AC   A7GN06;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   04-NOV-2026, entry version 98.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   OrderedLocusNames=Bcer98_1192 {ECO:0000313|EMBL:ABS21514.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21514.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS21514.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., Sanchis V.,
RA   Nguen-The C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714}.
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DR   EMBL; CP000764; ABS21514.1; -; Genomic_DNA.
DR   RefSeq; WP_011984267.1; NC_009674.1.
DR   AlphaFoldDB; A7GN06; -.
DR   STRING; 315749.Bcer98_1192; -.
DR   PaxDb; 315749-Bcer98_1192; -.
DR   GeneID; 33896543; -.
DR   KEGG; bcy:Bcer98_1192; -.
DR   eggNOG; COG0605; Bacteria.
DR   HOGENOM; CLU_031625_1_0_9; -.
DR   OMA; AAKMLQW; -.
DR   OrthoDB; 9803125at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.287.990:FF:000001; Superoxide dismutase; 1.
DR   FunFam; 3.55.40.20:FF:000004; Superoxide dismutase [Fe]; 1.
DR   Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR050265; Fe/Mn_Superoxide_Dismutase.
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   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABS21514.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002300}.
FT   DOMAIN          103..183
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          190..292
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
SQ   SEQUENCE   304 AA;  36519 MW;  B89A26A879DAA941 CRC64;
     MSQQGVFTDY FHEVESWCES VLDVLDSRAM EVYDVHMLAY KIQSLLERMK ENEYETDAEF
     LYEISEDVEH IQHHLQEVFM QEEEQCELYE RTYLDRSVPI GGHTLPPLPY PYHDLEPYIS
     REVMMLHHDK HHRSYVEGLN KAEKMMEEAR RTNKFDLIKH WEREAAFHGS GHYLHTIFWN
     NMKKDGGGSP RGELSEEIEK NFGSFLRFQK HFTEAASKVE GAGWAILVWV PRSGRLEILQ
     STLHQLFTQW DTVPLLVLDV WEHAYYLQYK NKKEEYIKNW WNVVNWPDVQ KRFEQAKQLE
     WIPY
//