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Database: UniProt
Entry: G2JC25_9BURK
LinkDB: G2JC25_9BURK
Original site: G2JC25_9BURK 
ID   G2JC25_9BURK            Unreviewed;       193 AA.
AC   G2JC25;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   16-JAN-2019, entry version 23.
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:CCD30331.1};
GN   ORFNames=CAGGBEG34_850002 {ECO:0000313|EMBL:CCD30331.1};
OS   Candidatus Glomeribacter gigasporarum BEG34.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Candidatus Glomeribacter.
OX   NCBI_TaxID=1070319 {ECO:0000313|EMBL:CCD30331.1};
RN   [1] {ECO:0000313|EMBL:CCD30331.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEG34 {ECO:0000313|EMBL:CCD30331.1};
RA   Ghignone S., Salvioli A., Anca I., Lumini E., Ortu G., Petiti L.,
RA   Cruveiller S., Bianciotto V., Piffanelli P., Lanfranco L.,
RA   Bonfante P.;
RT   "The genome of the obligate endobacterium of an arbuscular mycorrhizal
RT   fungus reveals an interphylum network of nutritional interactions.";
RL   Submitted (AUG-2011) 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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCD30331.1}.
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DR   EMBL; CAFB01000108; CCD30331.1; -; Genomic_DNA.
DR   RefSeq; WP_006683357.1; NZ_CAFB01000108.1.
DR   ProteinModelPortal; G2JC25; -.
DR   EnsemblBacteria; CCD30331; CCD30331; CAGGBEG34_850002.
DR   OrthoDB; 1440645at2; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CCD30331.1}.
FT   DOMAIN        3     81       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;  21535 MW;  F3993F1F02286FF6 CRC64;
     MTHILADLPY PKHALAPHIS EETLEYHYGK HHQSYVTTLN ALIPGTEFED LPLEAIIKKA
     SGPIFNNAAQ VWNHSFFWNC LTPQGAPSPG GALGDAIQRK WGAYDSFKEA FTKLALGTFG
     SGWAWLVRQA DGSLDLASTS NAGTPLTTAA KPLLTLDVWE HAYYIDYRNA RAKFIEAFWN
     IVNWAFAEQN FNH
//
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