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Database: UniProt/TrEMBL
Entry: A0A069B2N6_BURPE
LinkDB: A0A069B2N6_BURPE
Original site: A0A069B2N6_BURPE 
ID   A0A069B2N6_BURPE        Unreviewed;       192 AA.
AC   A0A069B2N6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-NOV-2017, entry version 31.
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:KGD57001.1};
GN   ORFNames=BOC41_08450 {ECO:0000313|EMBL:OSP96450.1}, BOC42_19125
GN   {ECO:0000313|EMBL:ARK89229.1}, DP46_818 {ECO:0000313|EMBL:AIO86484.1},
GN   DP49_3784 {ECO:0000313|EMBL:KGD57001.1}, ERS012350_04410
GN   {ECO:0000313|EMBL:CFL65687.1};
OS   Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=28450 {ECO:0000313|EMBL:KGD57001.1, ECO:0000313|Proteomes:UP000029527};
RN   [1] {ECO:0000313|EMBL:AIO86484.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=9 {ECO:0000313|EMBL:AIO86484.1};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S.,
RA   Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGD57001.1, ECO:0000313|Proteomes:UP000029527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BES {ECO:0000313|EMBL:KGD57001.1,
RC   ECO:0000313|Proteomes:UP000029527};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S.,
RA   Gu W., Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CFL65687.1, ECO:0000313|Proteomes:UP000047229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=109/96 {ECO:0000313|EMBL:CFL65687.1,
RC   ECO:0000313|Proteomes:UP000047229};
RG   Pathogen Informatics;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ARK89229.1, ECO:0000313|Proteomes:UP000193684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2008724734 {ECO:0000313|EMBL:ARK89229.1,
RC   ECO:0000313|Proteomes:UP000193684};
RA   Batra D.;
RT   "Burkholderia pseudomallei 2008724734.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:OSP96450.1, ECO:0000313|Proteomes:UP000193081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2008724644 {ECO:0000313|EMBL:OSP96450.1,
RC   ECO:0000313|Proteomes:UP000193081};
RA   Gee J.E., Gulvik C.A., Elrod M.D., Batra D., Rowe L.A., Sheth M.,
RA   Hoffmaster A.R.;
RT   "Phylogeography of Burkholderia pseudomallei isolates, Western
RT   Hemisphere.";
RL   Emerg. Infect. Dis. 0:0-0(2017).
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; CP008755; AIO86484.1; -; Genomic_DNA.
DR   EMBL; CP018380; ARK89229.1; -; Genomic_DNA.
DR   EMBL; CFWD01000014; CFL65687.1; -; Genomic_DNA.
DR   EMBL; JPHA01000231; KGD57001.1; -; Genomic_DNA.
DR   EMBL; NBVM01000001; OSP96450.1; -; Genomic_DNA.
DR   RefSeq; WP_004185841.1; NZ_NEGN01000324.1.
DR   EnsemblBacteria; CFU03619; CFU03619; ERS012314_05187.
DR   EnsemblBacteria; KGD57001; KGD57001; DP49_3784.
DR   EnsemblBacteria; KIX48564; KIX48564; SY87_07200.
DR   KEGG; but:X994_1856; -.
DR   PATRIC; fig|1435366.3.peg.2149; -.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   Proteomes; UP000029527; Unassembled WGS sequence.
DR   Proteomes; UP000047229; Unassembled WGS sequence.
DR   Proteomes; UP000193081; Unassembled WGS sequence.
DR   Proteomes; UP000193684; 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:UP000029527,
KW   ECO:0000313|Proteomes:UP000047229, ECO:0000313|Proteomes:UP000193081,
KW   ECO:0000313|Proteomes:UP000193684};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:KGD57001.1}.
FT   DOMAIN        3     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   192 AA;  21144 MW;  21741F7034DBAE59 CRC64;
     MAHTLPPLPY AEDALAPHIS QETIQFHYGK HHQAYVTNLN NLIPGTEFEN LPLEEIVKKS
     SGGIFNNAAQ IWNHTFFWNS LSPNGGGAPT GALGDAINAK WGSFDAFKEA FTKAAVGTFG
     SGWAWLVKKA DGSLDIVSTS NAATPLTTAD KPLVTIDVWE HAYYIDYRNA RPKFVEAFWN
     IVNWDFAAKN FA
//
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