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Database: UniProt/TrEMBL
Entry: A0A0A1FGP5_9BURK
LinkDB: A0A0A1FGP5_9BURK
Original site: A0A0A1FGP5_9BURK 
ID   A0A0A1FGP5_9BURK        Unreviewed;       192 AA.
AC   A0A0A1FGP5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   28-MAR-2018, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=LT85_3591 {ECO:0000313|EMBL:AIY42749.1};
OS   Collimonas arenae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY42749.1, ECO:0000313|Proteomes:UP000030302};
RN   [1] {ECO:0000313|EMBL:AIY42749.1, ECO:0000313|Proteomes:UP000030302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cal35 {ECO:0000313|EMBL:AIY42749.1,
RC   ECO:0000313|Proteomes:UP000030302};
RA   Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT   "Structure and function of bacterial communities in ageing soils:
RT   insights from the Mendocino ecological staircase.";
RL   Soil Biol. Biochem. 69:265-274(2014).
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; CP009962; AIY42749.1; -; Genomic_DNA.
DR   RefSeq; WP_038491441.1; NZ_CP009962.1.
DR   EnsemblBacteria; AIY42749; AIY42749; LT85_3591.
DR   KEGG; care:LT85_3591; -.
DR   KO; K04564; -.
DR   Proteomes; UP000030302; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000030302};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AIY42749.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030302}.
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;  21146 MW;  B8E20DFE98A9551E CRC64;
     MAHTLPPLPY ALDALAPHIS KETLEFHYGK HHQTYVTNLN NLIPGTEFEN LSLEDTVKKS
     SGGVFNNAAQ IWNHTFYWHS LSPNGGGAPT GALADAINAK WGSFDNFKVE LTKTAVGTFG
     SGWAWLVKNA DGSLGLVSTS NAATPLTTDA KPLITVDVWE HAYYIDYRNA RPKYLEAFWA
     LANWEFASQN FA
//
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