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Database: UniProt/TrEMBL
Entry: K7YQC2_BDEBC
LinkDB: K7YQC2_BDEBC
Original site: K7YQC2_BDEBC 
ID   K7YQC2_BDEBC            Unreviewed;       194 AA.
AC   K7YQC2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   07-JUN-2017, entry version 22.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodB {ECO:0000313|EMBL:AFY02041.1};
GN   ORFNames=Bdt_2358 {ECO:0000313|EMBL:AFY02041.1};
OS   Bdellovibrio bacteriovorus str. Tiberius.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=1069642 {ECO:0000313|EMBL:AFY02041.1, ECO:0000313|Proteomes:UP000010074};
RN   [1] {ECO:0000313|EMBL:AFY02041.1, ECO:0000313|Proteomes:UP000010074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tiberius {ECO:0000313|EMBL:AFY02041.1};
RX   PubMed=23181807; DOI=10.1186/1471-2164-13-670;
RA   Hobley L., Lerner T.R., Williams L.E., Lambert C., Till R.,
RA   Milner D.S., Basford S.M., Capeness M.J., Fenton A.K., Atterbury R.J.,
RA   Harris M.A., Sockett R.E.;
RT   "Genome analysis of a simultaneously predatory and prey-independent,
RT   novel Bdellovibrio bacteriovorus from the River Tiber, supports in
RT   silico predictions of both ancient and recent lateral gene transfer
RT   from diverse bacteria.";
RL   BMC Genomics 13:670-670(2012).
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; CP002930; AFY02041.1; -; Genomic_DNA.
DR   ProteinModelPortal; K7YQC2; -.
DR   EnsemblBacteria; AFY02041; AFY02041; Bdt_2358.
DR   KEGG; bbat:Bdt_2358; -.
DR   PATRIC; fig|1069642.3.peg.2332; -.
DR   KO; K04564; -.
DR   Proteomes; UP000010074; 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   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:UP000010074};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    190       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        75     75       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   194 AA;  21894 MW;  7E783822FB1C4F42 CRC64;
     MMNFELPALP YAKDALIPHM SAETLEYHHG KHHKTYVDNL NKLVPGTEHE GKTLEQIIMT
     SSGGVFNNAA QIWNHTFFWN CLSPNGGGEP AGELAQAIVR DFGSIEKFKE LFADASIKQF
     GSGWGWLVKN KEGKLEILST SNAETPMTKG HTAILTCDVW EHAYYIDYRN SRPNFLAAFW
     KLVNWEFAAK NFKA
//
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