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Database: UniProt/TrEMBL
Entry: G6Y314_9RHIZ
LinkDB: G6Y314_9RHIZ
Original site: G6Y314_9RHIZ 
ID   G6Y314_9RHIZ            Unreviewed;       198 AA.
AC   G6Y314;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   05-JUL-2017, entry version 23.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=MEA186_01548 {ECO:0000313|EMBL:EHH13808.1};
OS   Mesorhizobium amorphae CCNWGS0123.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=1082933 {ECO:0000313|EMBL:EHH13808.1, ECO:0000313|Proteomes:UP000002949};
RN   [1] {ECO:0000313|EMBL:EHH13808.1, ECO:0000313|Proteomes:UP000002949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCNWGS0123 {ECO:0000313|EMBL:EHH13808.1,
RC   ECO:0000313|Proteomes:UP000002949};
RX   PubMed=22247533; DOI=10.1128/JB.06475-11;
RA   Hao X., Lin Y., Johnstone L., Baltrus D.A., Miller S.J., Wei G.,
RA   Rensing C.;
RT   "Draft Genome Sequence of Plant Growth-Promoting Rhizobium
RT   Mesorhizobium amorphae, Isolated from Zinc-Lead Mine Tailings.";
RL   J. Bacteriol. 194:736-737(2012).
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; AGSN01000018; EHH13808.1; -; Genomic_DNA.
DR   RefSeq; WP_006199690.1; NZ_CP015318.1.
DR   EnsemblBacteria; EHH13808; EHH13808; MEA186_01548.
DR   GeneID; 32098834; -.
DR   KEGG; mamo:A6B35_12475; -.
DR   PATRIC; fig|1082933.3.peg.264; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000002949; 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   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   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:UP000002949};
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   198 AA;  22197 MW;  884B3489E62CC9A2 CRC64;
     MAFELPALPY DYEALQPYMS KETLEYHHDK HHKAYVDNGN KLAAEAGMGD LSVEDVVKQS
     FGKNAGLFNN AAQHYNHIHF WKWMKKGGGG NKLPGALQKA FDSDLGGYDK FKADFIAAGT
     TQFGSGWAWV SVKDGKLAIS KTPNGENPLV HGATPILGVD VWEHSYYIDY RNARPKYLEA
     FVDSLINWDH VLELYEKA
//
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