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Database: UniProt/TrEMBL
Entry: A0A0E0UA89_SINMB
LinkDB: A0A0E0UA89_SINMB
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ID   A0A0E0UA89_SINMB        Unreviewed;       200 AA.
AC   A0A0E0UA89;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=SinmeB_0587 {ECO:0000313|EMBL:AEG03526.1};
OS   Sinorhizobium meliloti (strain BL225C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=698936 {ECO:0000313|EMBL:AEG03526.1, ECO:0000313|Proteomes:UP000008709};
RN   [1] {ECO:0000313|Proteomes:UP000008709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL225C {ECO:0000313|Proteomes:UP000008709};
RX   PubMed=21569405; DOI=10.1186/1471-2164-12-235;
RG   US DOE Joint Genome Institute;
RA   Galardini M., Mengoni A., Brilli M., Pini F., Fioravanti A., Lucas S.,
RA   Lapidus A., Cheng J.F., Goodwin L., Pitluck S., Land M., Hauser L.,
RA   Woyke T., Mikhailova N., Ivanova N., Daligault H., Bruce D.,
RA   Detter C., Tapia R., Han C., Teshima H., Mocali S., Bazzicalupo M.,
RA   Biondi E.G.;
RT   "Exploring the symbiotic pangenome of the nitrogen-fixing bacterium
RT   Sinorhizobium meliloti.";
RL   BMC Genomics 12:235-235(2011).
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; CP002740; AEG03526.1; -; Genomic_DNA.
DR   RefSeq; WP_003537242.1; NC_017322.1.
DR   EnsemblBacteria; AEG03526; AEG03526; SinmeB_0587.
DR   KEGG; smq:SinmeB_0587; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; SMEL698936:GLK9-584-MONOMER; -.
DR   Proteomes; UP000008709; Chromosome.
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:UP000008709};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    191       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   200 AA;  22456 MW;  EF7F58A37933F73F CRC64;
     MAFELPNLPY DYDALAPYMS RETLEYHHDK HHLAYVTNGN KLAEEAGLSD LSLEDIVKKS
     YGTNQPLFNN AGQHYNHVHF WKWMKKGGGG TSLPGKLDAA IKSDLGGYDK FRADFIAAGA
     GQFGSGWAWL SVKNGKLEIS KTPNGENPLV HGATPILGVD VWEHSYYIDY RNARPKYLEA
     FVDNLINWDY VLELYEAAAK
//
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