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Database: UniProt
Entry: A0A246JG47_9BURK
LinkDB: A0A246JG47_9BURK
Original site: A0A246JG47_9BURK 
ID   A0A246JG47_9BURK        Unreviewed;       194 AA.
AC   A0A246JG47;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   16-JAN-2019, entry version 6.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=CDN99_10400 {ECO:0000313|EMBL:OWQ91543.1};
OS   Roseateles aquatilis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Roseateles.
OX   NCBI_TaxID=431061 {ECO:0000313|EMBL:OWQ91543.1, ECO:0000313|Proteomes:UP000197468};
RN   [1] {ECO:0000313|EMBL:OWQ91543.1, ECO:0000313|Proteomes:UP000197468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 48205 {ECO:0000313|EMBL:OWQ91543.1,
RC   ECO:0000313|Proteomes:UP000197468};
RX   PubMed=18175673; DOI=.1099/ijs.0.65169-0;
RA   Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT   "Description of Roseateles aquatilis sp. nov. and Roseateles terrae
RT   sp. nov., in the class Betaproteobacteria, and emended description of
RT   the genus Roseateles.";
RL   Int. J. Syst. Evol. Microbiol. 58:6-11(2008).
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:OWQ91543.1}.
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DR   EMBL; NIOF01000003; OWQ91543.1; -; Genomic_DNA.
DR   Proteomes; UP000197468; Unassembled WGS sequence.
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:UP000197468};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       89    190       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   194 AA;  21521 MW;  1E760BD5B659D105 CRC64;
     MEHVLPELPY DKKALEPHIS AETLEYHHGK HHKAYVDNLN NLQKGTEFES KTLEEIVKTS
     SGGIYNNAAQ IWNHTFFWSC LKPNGGGAPT GKLADAINAK WGSVDAFKEA FQKSAVGNFG
     SGWTWLVKKA DGSVDIVNMG AAGTPLTTGD TALLTIDVWE HAYYIDYRNA RPKFVETFLK
     SLVNWDFAQA NFGN
//
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