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Database: UniProt/TrEMBL
Entry: F7YYZ1_BACC6
LinkDB: F7YYZ1_BACC6
Original site: F7YYZ1_BACC6 
ID   F7YYZ1_BACC6            Unreviewed;       202 AA.
AC   F7YYZ1;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   07-JUN-2017, entry version 29.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:AEH53765.1};
GN   OrderedLocusNames=BCO26_1706 {ECO:0000313|EMBL:AEH53765.1};
OS   Bacillus coagulans (strain 2-6).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=941639 {ECO:0000313|EMBL:AEH53765.1, ECO:0000313|Proteomes:UP000005637};
RN   [1] {ECO:0000313|EMBL:AEH53765.1, ECO:0000313|Proteomes:UP000005637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-6 {ECO:0000313|EMBL:AEH53765.1,
RC   ECO:0000313|Proteomes:UP000005637};
RX   PubMed=21705584; DOI=10.1128/JB.05378-11;
RA   Su F., Yu B., Sun J., Ou H.Y., Zhao B., Wang L., Qin J., Tang H.,
RA   Tao F., Jarek M., Scharfe M., Ma C., Ma Y., Xu P.;
RT   "Genome sequence of the thermophilic strain Bacillus coagulans 2-6, an
RT   efficient producer of high-optical-purity L-lactic acid.";
RL   J. Bacteriol. 193:4563-4564(2011).
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; CP002472; AEH53765.1; -; Genomic_DNA.
DR   RefSeq; WP_013859658.1; NC_015634.1.
DR   EnsemblBacteria; AEH53765; AEH53765; BCO26_1706.
DR   GeneID; 29812583; -.
DR   KEGG; bck:BCO26_1706; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000005637; 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:UP000005637};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   202 AA;  22720 MW;  DEF501B5BA3A999A CRC64;
     MTYTLPQLPY AYDALEPYID KETMNIHHTK HHNTYVTNLN KALEGHDDLA SKSVEDLISD
     LNAVPEEIRT AVRNNGGGHA NHSLFWTLLS PNGGGEPKGA LLDAINSKFG SFEKFKEQFA
     AAAAGRFGSG WAWLVVHNGE LEIMSTPNQD SPLSEGKKPV LGLDVWEHAY YLKYQNRRPE
     YISAFWNVVN WDEVEKLYEA AK
//
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