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Database: UniProt/TrEMBL
Entry: A0A0M4NZE9_9BURK
LinkDB: A0A0M4NZE9_9BURK
Original site: A0A0M4NZE9_9BURK 
ID   A0A0M4NZE9_9BURK        Unreviewed;       192 AA.
AC   A0A0M4NZE9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AC233_14465 {ECO:0000313|EMBL:ALE55732.1};
OS   Burkholderia sp. HB1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1678678 {ECO:0000313|EMBL:ALE55732.1};
RN   [1] {ECO:0000313|EMBL:ALE55732.1, ECO:0000313|Proteomes:UP000055428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB1 {ECO:0000313|EMBL:ALE55732.1,
RC   ECO:0000313|Proteomes:UP000055428};
RX   PubMed=26543118;
RA   Ohtsubo Y., Moriya A., Kato H., Ogawa N., Nagata Y., Tsuda M.;
RT   "Complete Genome Sequence of a Phenanthrene Degrader, Burkholderia sp.
RT   HB-1 (NBRC 110738).";
RL   Genome Announc. 3:e01283-15(2015).
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; CP012192; ALE55732.1; -; Genomic_DNA.
DR   RefSeq; WP_006050063.1; NZ_CP012192.1.
DR   EnsemblBacteria; ALE55732; ALE55732; AC233_14465.
DR   KEGG; buq:AC233_14465; -.
DR   PATRIC; fig|1678678.3.peg.3127; -.
DR   KO; K04564; -.
DR   Proteomes; UP000055428; 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:UP000055428};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     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;  21418 MW;  BC7E66B949AAF1D4 CRC64;
     MEHTLPPLPF AKNALAPHMS EETLEFHYGK HHQTYVTNLN NLIKGTEFEN LSLEEIVKKS
     SGGVFNNAAQ VWNHTFFWNS LSPQGGGAPT GALADAINAK WGSFDKFKEE FAKTAIGTFG
     SGWAWLVKKA DGSLDLVSTS NAATPLTTDA KALITIDVWE HAYYIDYRNA RPKFVEAYWN
     IVNWEFASKN FA
//
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