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Database: UniProt/TrEMBL
Entry: G2TPL5_BACCO
LinkDB: G2TPL5_BACCO
Original site: G2TPL5_BACCO 
ID   G2TPL5_BACCO            Unreviewed;       202 AA.
AC   G2TPL5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 36.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Bcoa_2801 {ECO:0000313|EMBL:AEP01977.1};
OS   Bacillus coagulans 36D1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=345219 {ECO:0000313|EMBL:AEP01977.1, ECO:0000313|Proteomes:UP000009283};
RN   [1] {ECO:0000313|EMBL:AEP01977.1, ECO:0000313|Proteomes:UP000009283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36D1 {ECO:0000313|EMBL:AEP01977.1,
RC   ECO:0000313|Proteomes:UP000009283};
RX   PubMed=22675583; DOI=10.4056/sigs.2365342;
RA   Rhee M.S., Moritz B.E., Xie G., Glavina Del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Chertkov O., Brettin T., Han C., Detter C.,
RA   Pitluck S., Land M.L., Patel M., Ou M., Harbrucker R., Ingram L.O.,
RA   Shanmugam K.T.;
RT   "Complete Genome Sequence of a thermotolerant sporogenic lactic acid
RT   bacterium, Bacillus coagulans strain 36D1.";
RL   Stand. Genomic Sci. 5:331-340(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; CP003056; AEP01977.1; -; Genomic_DNA.
DR   RefSeq; WP_014098009.1; NC_016023.1.
DR   ProteinModelPortal; G2TPL5; -.
DR   STRING; 345219.Bcoa_2801; -.
DR   EnsemblBacteria; AEP01977; AEP01977; Bcoa_2801.
DR   KEGG; bag:Bcoa_2801; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000009283; 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:UP000009283};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009283}.
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;  22708 MW;  DEF0A4309BCE59AA CRC64;
     MTYTLPQLPY AYDALEPYID KETMNIHHTK HHNTYVTNLN KALEGHDDLA SKSVEDLISD
     LNAVPEEIRT AVRNNGGGHA NHSLFWTLLS PNGGGEPKGA LLDAINSKFG SFEKFKEQFA
     AAAAGRFGSG WAWLVVNNGE LEITSTPNQD NPLSEGKKPI LGLDVWEHAY YLKYQNRRPE
     YISAFWNVVN WDEVEKLYEA AK
//
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