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Database: UniProt/TrEMBL
Entry: A9VH58_BACWK
LinkDB: A9VH58_BACWK
Original site: A9VH58_BACWK 
ID   A9VH58_BACWK            Unreviewed;       203 AA.
AC   A9VH58;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=BcerKBAB4_4128 {ECO:0000313|EMBL:ABY45290.1};
OS   Bacillus weihenstephanensis (strain KBAB4).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730 {ECO:0000313|EMBL:ABY45290.1, ECO:0000313|Proteomes:UP000002154};
RN   [1] {ECO:0000313|EMBL:ABY45290.1, ECO:0000313|Proteomes:UP000002154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4 {ECO:0000313|EMBL:ABY45290.1,
RC   ECO:0000313|Proteomes:UP000002154};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA   Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H.,
RA   Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P.,
RA   Weissenbach J., 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   -!- 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; CP000903; ABY45290.1; -; Genomic_DNA.
DR   RefSeq; WP_001052029.1; NC_010184.1.
DR   ProteinModelPortal; A9VH58; -.
DR   STRING; 315730.BcerKBAB4_4128; -.
DR   EnsemblBacteria; ABY45290; ABY45290; BcerKBAB4_4128.
DR   GeneID; 29401952; -.
DR   KEGG; bwe:BcerKBAB4_4128; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   Proteomes; UP000002154; 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 {ECO:0000313|Proteomes:UP000002154};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:ABY45290.1}.
FT   DOMAIN        3     91       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    197       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;  22591 MW;  D1E638904A1D473A CRC64;
     MAKHELPNLP YAYDALEPHF DKETMNIHHT KHHNTYITNL NAALEGHAEL ADKSVEELVA
     NLNEVPEAIR TAVRNNGGGH ANHTFFWTIL SPNGGGQPVG ELATAIEAKF GSFDAFKAEF
     AKAGATRFGS GWAWLVVNNG ELEVTSTPNQ DSPLTEGKTP VIGLDVWEHA YYLNYQNRRP
     DYIGAFWNVV DWNVAEKLYQ EAK
//
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