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Database: UniProt/TrEMBL
Entry: S6A350_BACPJ
LinkDB: S6A350_BACPJ
Original site: S6A350_BACPJ 
ID   S6A350_BACPJ            Unreviewed;       204 AA.
AC   S6A350;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   25-OCT-2017, entry version 23.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=M493_12775 {ECO:0000313|EMBL:AGT32801.1};
OS   Bacillus sp. (strain JF8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1921421 {ECO:0000313|EMBL:AGT32801.1, ECO:0000313|Proteomes:UP000015500};
RN   [1] {ECO:0000313|EMBL:AGT32801.1, ECO:0000313|Proteomes:UP000015500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF8 {ECO:0000313|EMBL:AGT32801.1,
RC   ECO:0000313|Proteomes:UP000015500};
RX   PubMed=24459274;
RA   Shintani M., Ohtsubo Y., Fukuda K., Hosoyama A., Ohji S., Yamazoe A.,
RA   Fujita N., Nagata Y., Tsuda M., Hatta T., Kimbara K.;
RT   "Complete Genome Sequence of the Thermophilic Polychlorinated Biphenyl
RT   Degrader Geobacillus sp. Strain JF8 (NBRC 109937).";
RL   Genome Announc. 2:e01213-13(2014).
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; CP006254; AGT32801.1; -; Genomic_DNA.
DR   RefSeq; WP_020960593.1; NC_022080.4.
DR   EnsemblBacteria; AGT32801; AGT32801; M493_12775.
DR   KEGG; gjf:M493_12775; -.
DR   PATRIC; fig|1345697.3.peg.2487; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000015500; 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:UP000015500};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     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   204 AA;  22770 MW;  8642C6B7EB914DEA CRC64;
     MPFELPALPY AYDALEPHID KETMNIHHTK HHNTYVTNLN AALEGQADLQ NKSLEELLSN
     LEALPESIRT AVRNNGGGHA NHSLFWTILS PNGGGEPTGE LADAINQKFG SFAAFKDEFS
     KAAAGRFGSG WAWLVVNNGE LEITSTPNQD SPIMEGKTPI LGLDVWEHAY YLKYQNRRPE
     YIAAFWNVVN WDEVAKRYSE AKAK
//
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