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Database: UniProt/TrEMBL
Entry: R9TYB2_9BACI
LinkDB: R9TYB2_9BACI
Original site: R9TYB2_9BACI 
ID   R9TYB2_9BACI            Unreviewed;       203 AA.
AC   R9TYB2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-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   Name=sodA {ECO:0000313|EMBL:AGN37115.1};
GN   ORFNames=BaLi_c27670 {ECO:0000313|EMBL:AGN37115.1};
OS   Bacillus paralicheniformis ATCC 9945a.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=766760 {ECO:0000313|EMBL:AGN37115.1, ECO:0000313|Proteomes:UP000014068};
RN   [1] {ECO:0000313|EMBL:AGN37115.1, ECO:0000313|Proteomes:UP000014068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9945A {ECO:0000313|Proteomes:UP000014068};
RX   PubMed=23908277;
RA   Rachinger M., Volland S., Meinhardt F., Daniel R., Liesegang H.;
RT   "First Insights into the Completely Annotated Genome Sequence of
RT   Bacillus licheniformis Strain 9945A.";
RL   Genome Announc. 1:e00525-13(2013).
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; CP005965; AGN37115.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGN37115; AGN37115; BaLi_c27670.
DR   KEGG; blh:BaLi_c27670; -.
DR   PATRIC; fig|766760.3.peg.2861; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000014068; 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:UP000014068};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AGN37115.1}.
FT   DOMAIN        3     91       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        83     83       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  22661 MW;  E152607C72C02888 CRC64;
     MMAYKLPELP YAYDALEPHI DKETMNIHHT KHHNTYVTKL NEAVAGKQDL ESKSVEELVA
     NLDAVPENIR SAVRNNGGGH ANHSLFWKLL SPNGGGAPTG ELAEAINSKF GSFDQFKEDF
     AAAAAGRFGS GWAWLVVNNG ELEITSTPNQ DSPLSEGKTP ILGLDVWEHA YYLNYQNRRP
     DYIKAFWNVV NWDEVARLYS EAK
//
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