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Database: UniProt/TrEMBL
Entry: A0A0E1CRP1_KLEPN
LinkDB: A0A0E1CRP1_KLEPN
Original site: A0A0E1CRP1_KLEPN 
ID   A0A0E1CRP1_KLEPN        Unreviewed;       216 AA.
AC   A0A0E1CRP1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-MAR-2018, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=KPNJ1_05380 {ECO:0000313|EMBL:AHM87768.1};
OS   Klebsiella pneumoniae 30660/NJST258_1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1420012 {ECO:0000313|EMBL:AHM87768.1, ECO:0000313|Proteomes:UP000019583};
RN   [1] {ECO:0000313|EMBL:AHM87768.1, ECO:0000313|Proteomes:UP000019583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30660/NJST258_1 {ECO:0000313|EMBL:AHM87768.1,
RC   ECO:0000313|Proteomes:UP000019583};
RX   PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA   Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA   Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J.,
RA   Bonomo R.A., Musser J.M., Kreiswirth B.N.;
RT   "Molecular dissection of the evolution of carbapenem-resistant
RT   multilocus sequence type 258 Klebsiella pneumoniae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
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; CP006923; AHM87768.1; -; Genomic_DNA.
DR   EnsemblBacteria; AHM87768; AHM87768; KPNJ1_05380.
DR   KEGG; kpa:KPNJ1_05380; -.
DR   PATRIC; fig|1420012.3.peg.5016; -.
DR   KO; K04564; -.
DR   Proteomes; UP000019583; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
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:UP000019583};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AHM87768.1}.
FT   DOMAIN       12     99       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      106    211       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        37     37       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        92     92       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       178    178       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       182    182       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   216 AA;  24165 MW;  3EB30641187F98D3 CRC64;
     MSRSTIMEMI MSYTLPSLPY AYDALEPHFD KQTMEIHHTK HHQTYVNNAN AALESLPEFA
     NLSAEELITK LDQLPADKKT VLRNNAGGHA NHSLFWKGLK TGTTLQGDLK AAIERDFGSV
     ENFKAEFEKA AATRFGSGWA WLVLKGDKLA VVSTANQDSP LMGEAISGAS GFPIIGLDVW
     EHAYYLKFQN RRPDYIKAFW DVVNWDEAAA RFAAKK
//
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