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Database: UniProt/TrEMBL
Entry: F7Y8N2_MESOW
LinkDB: F7Y8N2_MESOW
Original site: F7Y8N2_MESOW 
ID   F7Y8N2_MESOW            Unreviewed;       199 AA.
AC   F7Y8N2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   07-JUN-2017, entry version 30.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Mesop_5417 {ECO:0000313|EMBL:AEH89833.1};
OS   Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH89833.1, ECO:0000313|Proteomes:UP000001623};
RN   [1] {ECO:0000313|EMBL:AEH89833.1, ECO:0000313|Proteomes:UP000001623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24607 / HAMBI 3007 / WSM2075
RC   {ECO:0000313|Proteomes:UP000001623};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M.,
RA   Tiwari R.P., Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium opportunistum WSM2075.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002279; AEH89833.1; -; Genomic_DNA.
DR   RefSeq; WP_013896470.1; NC_015675.1.
DR   STRING; 536019.Mesop_5417; -.
DR   EnsemblBacteria; AEH89833; AEH89833; Mesop_5417.
DR   KEGG; mop:Mesop_5417; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000001623; 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   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:UP000001623};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AEH89833.1}.
FT   DOMAIN        3     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    192       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   199 AA;  22277 MW;  C0799155E35190C2 CRC64;
     MAFELPALPY DYEALQPYMS KETLEYHHDK HHKAYVDNGN KLAAEAGLGD LSVEEVVKQS
     FGKNAGLFNN AAQHYNHIHF WKWMKKGGGG NKLPGALQKA VDSDLGGYDK FKADFIAAGT
     TQFGSGWAWV SVKDGKLAIS KTPNGENPLV HGASPILGVD VWEHSYYIDY RNARPKYLEA
     FVDSLINWDH VLEMYEKAK
//
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