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Database: UniProt/TrEMBL
Entry: A0A1L3MPU4_9BACI
LinkDB: A0A1L3MPU4_9BACI
Original site: A0A1L3MPU4_9BACI 
ID   A0A1L3MPU4_9BACI        Unreviewed;       202 AA.
AC   A0A1L3MPU4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-SEP-2017, entry version 5.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=A9C19_06210 {ECO:0000313|EMBL:APH04371.1};
OS   Bacillus weihaiensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH04371.1, ECO:0000313|Proteomes:UP000181936};
RN   [1] {ECO:0000313|EMBL:APH04371.1, ECO:0000313|Proteomes:UP000181936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alg07 {ECO:0000313|EMBL:APH04371.1,
RC   ECO:0000313|Proteomes:UP000181936};
RX   PubMed=27901120; DOI=10.1038/srep38248;
RA   Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT   "Complete genome sequence and transcriptomic analysis of a novel
RT   marine strain Bacillus weihaiensis reveals the mechanism of brown
RT   algae degradation.";
RL   Sci. Rep. 6:38248-38248(2016).
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; CP016020; APH04371.1; -; Genomic_DNA.
DR   RefSeq; WP_072579162.1; NZ_CP016020.1.
DR   KEGG; bwh:A9C19_06210; -.
DR   KO; K04564; -.
DR   Proteomes; UP000181936; 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:UP000181936};
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:UP000181936}.
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   202 AA;  22522 MW;  04C77A970B67FA99 CRC64;
     MAYELPQLPY AYDALEPHID KETMNIHHTK HHNTYITNVN GALEGHADLA SKSVEELVSN
     LDAVPEAIRP AVRNNGGGHA NHSLFWSILS PNGGGEPTGE LADAITAKFG SYDNFKEEFA
     KAATTRFGSG WAWLVVNNGE IEVTSTPNQD SPLMEGKTPI LGLDVWEHAY YLNYQNRRPD
     YISSFWNVVN WDEVSKRYTS AK
//
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