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Database: UniProt
Entry: A0A0S6UK23_9BRAD
LinkDB: A0A0S6UK23_9BRAD
Original site: A0A0S6UK23_9BRAD 
ID   A0A0S6UK23_9BRAD        Unreviewed;       198 AA.
AC   A0A0S6UK23;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   18-JUL-2018, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BDOA9_0104060 {ECO:0000313|EMBL:GAJ31229.1};
OS   Bradyrhizobium sp. DOA9.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ31229.1, ECO:0000313|Proteomes:UP000066441};
RN   [1] {ECO:0000313|EMBL:GAJ31229.1, ECO:0000313|Proteomes:UP000066441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOA9 {ECO:0000313|EMBL:GAJ31229.1,
RC   ECO:0000313|Proteomes:UP000066441};
RX   PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA   Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA   Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA   Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT   "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a
RT   Symbiotic Plasmid.";
RL   PLoS ONE 10:e0117392-e0117392(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; DF820425; GAJ31229.1; -; Genomic_DNA.
DR   RefSeq; WP_025032276.1; NZ_DF820425.1.
DR   Proteomes; UP000066441; 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:UP000066441};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   198 AA;  22549 MW;  391FE9138A58FEEF CRC64;
     MTFTLPPLPY AYDALGQYMS KETLEYHHDK HHQAYVTNGN NALKGTEWEG KSLEEIVKGS
     FGKNPAVFNN AGQHYNHIHF WNWMKPNGGG TKLPGKIEKK INEDLGGFEK FKADFQAAGV
     GQFGSGWAWL QVKNGKLEIS KTPNGENPLV HGATPILGVD VWEHSYYIDY RNRRPDYLKA
     FVENLVNWEY VESLFEKA
//
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