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Database: UniProt/TrEMBL
Entry: A0A0B6S2G4_BURGL
LinkDB: A0A0B6S2G4_BURGL
Original site: A0A0B6S2G4_BURGL 
ID   A0A0B6S2G4_BURGL        Unreviewed;       219 AA.
AC   A0A0B6S2G4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
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:AJK47525.1};
GN   ORFNames=BGL_1c30490 {ECO:0000313|EMBL:AJK47525.1};
OS   Burkholderia glumae PG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=595500 {ECO:0000313|EMBL:AJK47525.1, ECO:0000313|Proteomes:UP000031838};
RN   [1] {ECO:0000313|Proteomes:UP000031838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1 {ECO:0000313|Proteomes:UP000031838};
RA   Voget S., Streit W.R., Jaeger K.E., Daniel R.;
RL   Submitted (MAR-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: 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; CP002580; AJK47525.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJK47525; AJK47525; BGL_1c30490.
DR   KEGG; bgp:BGL_1c30490; -.
DR   KO; K04564; -.
DR   Proteomes; UP000031838; Chromosome 1.
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:UP000031838};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AJK47525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031838}.
FT   DOMAIN       30    109       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      116    216       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        54     54       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       101    101       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       184    184       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       188    188       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   219 AA;  24071 MW;  B935B93E42888372 CRC64;
     MRGYSVSPTI GRSAGPSPYT YTSKESVMAH TLPPLPYSED ALAPHISQET IQFHYGKHHQ
     TYVTNLNNLI PGTEFENLSL EETVKKSSGG IFNNAAQIWN HTFFWNSLSP NGGGAPTGAL
     GDAINAKWGS FDAFKEAFAK TAIGTFGSGW AWLVKKADGS LDLVSTSNAA TPLTTDAKPL
     LTIDVWEHAY YIDYRNARPK FVEAFWNVVN WDFAAKNFV
//
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