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Database: UniProt/TrEMBL
Entry: A0A0H3EHV1_ECO8N
LinkDB: A0A0H3EHV1_ECO8N
Original site: A0A0H3EHV1_ECO8N 
ID   A0A0H3EHV1_ECO8N        Unreviewed;       193 AA.
AC   A0A0H3EHV1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=NRG857_08300 {ECO:0000313|EMBL:ADR27084.1};
OS   Escherichia coli O83:H1 (strain NRG 857C / AIEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=685038 {ECO:0000313|EMBL:ADR27084.1, ECO:0000313|Proteomes:UP000008614};
RN   [1] {ECO:0000313|EMBL:ADR27084.1, ECO:0000313|Proteomes:UP000008614}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRG 857C / AIEC {ECO:0000313|Proteomes:UP000008614};
RX   PubMed=21108814; DOI=10.1186/1471-2164-11-667;
RA   Nash J.H., Villegas A., Kropinski A.M., Aguilar-Valenzuela R.,
RA   Konczy P., Mascarenhas M., Ziebell K., Torres A.G., Karmali M.A.,
RA   Coombes B.K.;
RT   "Genome sequence of adherent-invasive Escherichia coli and comparative
RT   genomic analysis with other E. coli pathotypes.";
RL   BMC Genomics 11:667-667(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; CP001855; ADR27084.1; -; Genomic_DNA.
DR   RefSeq; WP_000007283.1; NC_017634.1.
DR   RefSeq; YP_006120018.1; NC_017634.1.
DR   ProteinModelPortal; A0A0H3EHV1; -.
DR   SMR; A0A0H3EHV1; -.
DR   EnsemblBacteria; ADR27084; ADR27084; NRG857_08300.
DR   GeneID; 12875281; -.
DR   KEGG; eln:NRG857_08300; -.
DR   PATRIC; fig|685038.3.peg.1673; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   Proteomes; UP000008614; 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:UP000008614};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
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;  21266 MW;  91236D2A8FE61474 CRC64;
     MSFELPALPY AKDALAPHIS AETIEYHYGK HHQTYVTNLN NLIKGTAFEG KSLEEIIRSS
     EGGVFNNAAQ VWNHTFYWNC LAPNAGGEPT GKVAEAIAAS FGSFADFKAQ FTDAAIKNFG
     SGWTWLVKNS DGKLAIVSTS NAGTPLTTDA TPLLTVDVWE HAYYIDYRNA RPGYLEHFWA
     LVNWEFVAKN LAA
//
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