ID C6UVZ7_ECO5T Unreviewed; 193 AA.
AC C6UVZ7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 29-MAY-2013, entry version 31.
DE RecName: Full=Superoxide dismutase;
DE EC=1.15.1.1;
GN Name=sodB; OrderedLocusNames=ECSP_2222;
OS Escherichia coli O157:H7 (strain TW14359 / EHEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=544404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW14359 / EHEC;
RX PubMed=19564389; DOI=10.1128/IAI.00198-09;
RA Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E.,
RA Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M.,
RA Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J.,
RA Beskhlebnaya V., Waldor M.K., Samadpour M., Whittam T.S., Kaul R.,
RA Brittnacher M., Miller S.I.;
RT "Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-
RT associated outbreak isolate indicates candidate genes that may enhance
RT virulence.";
RL Infect. Immun. 77:3713-3721(2009).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems (By similarity).
CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001368; ACT72035.1; -; Genomic_DNA.
DR RefSeq; YP_003078111.1; NC_013008.1.
DR ProteinModelPortal; C6UVZ7; -.
DR SMR; C6UVZ7; 2-193.
DR STRING; 544404.ECSP_2222; -.
DR PRIDE; C6UVZ7; -.
DR EnsemblBacteria; ACT72035; ACT72035; ECSP_2222.
DR GeneID; 8216788; -.
DR KEGG; etw:ECSP_2222; -.
DR PATRIC; 18388454; VBIEscCol9396_2274.
DR eggNOG; COG0605; -.
DR HOGENOM; HOG000013584; -.
DR KO; K04564; -.
DR OMA; NCMAPNG; -.
DR ProtClustDB; PRK10543; -.
DR BioCyc; ECOL544404:GKCX-2221-MONOMER; -.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:EC.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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 PANTHER; PTHR11404; PTHR11404; 1.
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; SODismutase; 1.
DR SUPFAM; SSF54719; SODismutase; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Complete proteome; Oxidoreductase.
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
//