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Database: UniProt/TrEMBL
Entry: Q475F4_CUPNJ
LinkDB: Q475F4_CUPNJ
Original site: Q475F4_CUPNJ 
ID   Q475F4_CUPNJ            Unreviewed;       193 AA.
AC   Q475F4;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   25-OCT-2017, entry version 82.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Reut_A0597 {ECO:0000313|EMBL:AAZ59979.1};
OS   Cupriavidus necator (strain JMP 134 / LMG 1197) (Ralstonia eutropha
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ59979.1, ECO:0000313|Proteomes:UP000002697};
RN   [1] {ECO:0000313|Proteomes:UP000002697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197 {ECO:0000313|Proteomes:UP000002697};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000090; AAZ59979.1; -; Genomic_DNA.
DR   RefSeq; WP_011296785.1; NC_007347.1.
DR   ProteinModelPortal; Q475F4; -.
DR   STRING; 264198.Reut_A0597; -.
DR   EnsemblBacteria; AAZ59979; AAZ59979; Reut_A0597.
DR   KEGG; reu:Reut_A0597; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; REUT264198:G12XR-601-MONOMER; -.
DR   Proteomes; UP000002697; Chromosome 1.
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:UP000002697};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AAZ59979.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002697}.
FT   DOMAIN        2     82       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   193 AA;  21664 MW;  29256150AD6C2B5E CRC64;
     MEHKLPPLPY AHDALAPHIS KETLEFHHDK HHQTYVTNLN NLIKGTEFEN ATLEEITKKS
     SGGIFNNAAQ VWNHTFYWES MKPNGGGQPT GALADAINAK WGSFDKFKEE FTKTAVGTFG
     SGWAWLVKKA DGSLDLLSTS NAATPLTTDA KPLLTCDVWE HAYYIDYRNA RPKYVEAFWN
     VVNWDFAAQN FAG
//
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