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Database: UniProt/TrEMBL
Entry: M4UWR7_RALSL
LinkDB: M4UWR7_RALSL
Original site: M4UWR7_RALSL 
ID   M4UWR7_RALSL            Unreviewed;       192 AA.
AC   M4UWR7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   25-OCT-2017, entry version 28.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=F504_2472 {ECO:0000313|EMBL:AGH84985.1};
OS   Ralstonia solanacearum FQY_4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=1262456 {ECO:0000313|EMBL:AGH84985.1, ECO:0000313|Proteomes:UP000011880};
RN   [1] {ECO:0000313|EMBL:AGH84985.1, ECO:0000313|Proteomes:UP000011880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FQY_4 {ECO:0000313|EMBL:AGH84985.1,
RC   ECO:0000313|Proteomes:UP000011880};
RX   PubMed=23661471;
RA   Cao Y., Tian B., Liu Y., Cai L., Wang H., Lu N., Wang M., Shang S.,
RA   Luo Z., Shi J.;
RT   "Genome Sequencing of Ralstonia solanacearum FQY_4, Isolated from a
RT   Bacterial Wilt Nursery Used for Breeding Crop Resistance.";
RL   Genome Announc. 1:E00125-13(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; CP004012; AGH84985.1; -; Genomic_DNA.
DR   RefSeq; WP_011002442.1; NC_020799.1.
DR   ProteinModelPortal; M4UWR7; -.
DR   EnsemblBacteria; AGH84985; AGH84985; F504_2472.
DR   GeneID; 1221373; -.
DR   KEGG; rse:F504_2472; -.
DR   PATRIC; fig|1262456.3.peg.2489; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000011880; 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:UP000011880};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AGH84985.1}.
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;  21269 MW;  5FB96CBB28ABF110 CRC64;
     MAHTLPPLPY ALDALAPHIS KETLEFHYGK HHQTYVTNLN NLIPGTEFEN LSLEDIVKKS
     SGGLFNNAAQ VWNHTFYWNG LKPNGGGAPA GALADAINAK WGSFDKFKEE FTKVAIGTFG
     SGWAWLVKKA DGSLDLVSTS NAATPLTTDA KPLLTCDVWE HAYYIDYRNA RPKYVEAFWS
     LVNWDFVASN FA
//
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