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Database: UniProt
Entry: U6E289_9MOLU
LinkDB: U6E289_9MOLU
Original site: U6E289_9MOLU 
ID   U6E289_9MOLU            Unreviewed;       203 AA.
AC   U6E289;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   16-JAN-2019, entry version 28.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:CCP88167.1};
GN   ORFNames=S284_02300 {ECO:0000313|EMBL:CCP88167.1};
OS   Candidatus Phytoplasma solani.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=69896 {ECO:0000313|EMBL:CCP88167.1};
RN   [1] {ECO:0000313|EMBL:CCP88167.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=284/09 {ECO:0000313|EMBL:CCP88167.1};
RX   PubMed=24158016;
RA   Mitrovic J., Siewert C., Duduk B., Hecht J., Moelling K., Broecker F.,
RA   Beyerlein P., Buettner C., Bertaccini A., Kube M.;
RT   "Generation and analysis of draft sequences of 'stolbur' phytoplasma
RT   from multiple displacement amplification templates.";
RL   J. Mol. Microbiol. Biotechnol. 24:1-11(2014).
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}.
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DR   EMBL; FO393427; CCP88167.1; -; Genomic_DNA.
DR   EnsemblBacteria; CCP88167; CCP88167; S284_02300.
DR   KEGG; psol:S284_02300; -.
DR   PATRIC; fig|1273548.3.peg.347; -.
DR   KO; K04564; -.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   COILED       36     56       {ECO:0000256|SAM:Coils}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   203 AA;  23659 MW;  456B761C86CE4212 CRC64;
     MQFSLPKLNF KYDALEPFFD AKTMEIHHTK HHQTYINNLN DALKQHQQIN LTLEQMLTNL
     SLLPKDIRQI VRNNGGGHFN HTFFWTLLKL NHGILPQGLL EELINRDFGS LEGFKNAFAN
     IAKTIFGSGW AWMIINPKGH LEVTSTPNQD VVLDQGIPLI GLDVWEHAYY LNYQNRRIDY
     IEAFFNVLDW QQVATNLKNN YHV
//
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