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Database: UniProt/TrEMBL
Entry: D8NZE6_RALSL
LinkDB: D8NZE6_RALSL
Original site: D8NZE6_RALSL 
ID   D8NZE6_RALSL            Unreviewed;       192 AA.
AC   D8NZE6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   25-OCT-2017, entry version 37.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:CBJ50299.1};
GN   ORFNames=RPSI07_0939 {ECO:0000313|EMBL:CBJ50299.1};
OS   Ralstonia solanacearum PSI07.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=859657 {ECO:0000313|EMBL:CBJ50299.1, ECO:0000313|Proteomes:UP000006858};
RN   [1] {ECO:0000313|EMBL:CBJ50299.1, ECO:0000313|Proteomes:UP000006858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSI07 {ECO:0000313|EMBL:CBJ50299.1,
RC   ECO:0000313|Proteomes:UP000006858};
RX   PubMed=20550686; DOI=10.1186/1471-2164-11-379;
RA   Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E.,
RA   Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G.,
RA   Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.;
RT   "Genomes of three tomato pathogens within the Ralstonia solanacearum
RT   species complex reveal significant evolutionary divergence.";
RL   BMC Genomics 11:379-379(2010).
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; FP885906; CBJ50299.1; -; Genomic_DNA.
DR   RefSeq; WP_013211645.1; NC_014311.1.
DR   EnsemblBacteria; CBJ50299; CBJ50299; RPSI07_0939.
DR   KEGG; rsl:RPSI07_0939; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000006858; 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:UP000006858};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CBJ50299.1}.
FT   DOMAIN        3     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    189       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       157    157       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21376 MW;  0C986E7AD393EBCB CRC64;
     MAHTLPPLPY ALDALAPHIS KETLEFHYGK HHQTYVTNLN NLIPGTEFEN LSLEDIVKKS
     SGGIFNNAAQ VWNHTFYWNG LKPNGGGAPT GALADAINAK WGSFDKFKEE FTKVAIGTFG
     SGWAWLVKKA DGSLDLVSTS NAATPLTTDA KPLLTCDVWE HAYYIDYRNA RPKYVEAFWN
     LVNWDFVANH FA
//
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