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Database: UniProt/TrEMBL
Entry: A0A0A8JLT9_BACSX
LinkDB: A0A0A8JLT9_BACSX
Original site: A0A0A8JLT9_BACSX 
ID   A0A0A8JLT9_BACSX        Unreviewed;       200 AA.
AC   A0A0A8JLT9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=OXB_2905 {ECO:0000313|EMBL:BAQ11376.1};
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ11376.1, ECO:0000313|Proteomes:UP000031651};
RN   [1] {ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL   Submitted (AUG-2013) 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; AP013294; BAQ11376.1; -; Genomic_DNA.
DR   RefSeq; WP_041075185.1; NZ_AP013294.1.
DR   EnsemblBacteria; BAQ11376; BAQ11376; OXB_2905.
DR   KEGG; baco:OXB_2905; -.
DR   KO; K04564; -.
DR   Proteomes; UP000031651; 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:UP000031651};
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:UP000031651}.
FT   DOMAIN        2     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    197       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   200 AA;  22521 MW;  78B519586B59D838 CRC64;
     MAYTLPELPY AYDALEPHID KETMNIHHTK HHNTYITNLN NALEGNDELL SKSIEELISD
     MDAIPEDKRT AVRNNGGGHA NHSFFWQILS PNGGGNPSGA LAEAIDKKFG SFDAFKEEFA
     KAGATRFGSG WAWLVLNNGE LEVMSTANQD SPLMEGKTPL LGLDVWEHAY YLNYQNRRPD
     YISAFWNVVN WDEVAKRYGK
//
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