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Database: UniProt/TrEMBL
Entry: R9VQF3_9ENTR
LinkDB: R9VQF3_9ENTR
Original site: R9VQF3_9ENTR 
ID   R9VQF3_9ENTR            Unreviewed;       206 AA.
AC   R9VQF3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   25-OCT-2017, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=H650_15565 {ECO:0000313|EMBL:AGN86501.1};
OS   Enterobacter sp. R4-368.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=1166130 {ECO:0000313|EMBL:AGN86501.1, ECO:0000313|Proteomes:UP000014269};
RN   [1] {ECO:0000313|EMBL:AGN86501.1, ECO:0000313|Proteomes:UP000014269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R4-368 {ECO:0000313|EMBL:AGN86501.1};
RX   PubMed=23908287;
RA   Madhaiyan M., Peng N., Ji L.;
RT   "Complete Genome Sequence of Enterobacter sp. Strain R4-368, an
RT   Endophytic N-Fixing Gammaproteobacterium Isolated from Surface-
RT   Sterilized Roots of Jatropha curcas L.";
RL   Genome Announc. 1:e00544-13(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; CP005991; AGN86501.1; -; Genomic_DNA.
DR   RefSeq; WP_020455923.1; NC_021500.1.
DR   EnsemblBacteria; AGN86501; AGN86501; H650_15565.
DR   KEGG; enr:H650_15565; -.
DR   PATRIC; fig|1166130.5.peg.2979; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; ESP1166130:G135U-2971-MONOMER; -.
DR   Proteomes; UP000014269; 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:UP000014269};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    201       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       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   206 AA;  23050 MW;  9279D5FD188977D0 CRC64;
     MSYTLPALPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA SLPVEELITK
     LDQLPADKKT VLRNNAGGHA NHSLFWKGLK KGTTLQGDLK AAIERDFGSV DNFKAEFEKA
     AATRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GFPILGLDVW EHAYYLKFQN
     RRPDYIKEFW NVVNWDEAAA RFAAKK
//
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