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Database: UniProt/TrEMBL
Entry: A0A1Q2CUY3_9ACTN
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Original site: A0A1Q2CUY3_9ACTN 
ID   A0A1Q2CUY3_9ACTN        Unreviewed;       221 AA.
AC   A0A1Q2CUY3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   25-OCT-2017, entry version 6.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BW733_02765 {ECO:0000313|EMBL:AQP49914.1};
OS   Tessaracoccus flavescens.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Tessaracoccus.
OX   NCBI_TaxID=399497 {ECO:0000313|EMBL:AQP49914.1, ECO:0000313|Proteomes:UP000188235};
RN   [1] {ECO:0000313|EMBL:AQP49914.1, ECO:0000313|Proteomes:UP000188235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SST-39T {ECO:0000313|EMBL:AQP49914.1,
RC   ECO:0000313|Proteomes:UP000188235};
RX   PubMed=18398170; DOI=10.1099/ijs.0.64868-0;
RA   Lee D.W., Lee S.D.;
RT   "Tessaracoccus flavescens sp. nov., isolated from marine sediment.";
RL   Int. J. Syst. Evol. Microbiol. 58:785-789(2008).
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; CP019607; AQP49914.1; -; Genomic_DNA.
DR   KEGG; tfa:BW733_02765; -.
DR   KO; K04564; -.
DR   Proteomes; UP000188235; 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:UP000188235};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188235}.
FT   DOMAIN       20    101       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      108    210       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        45     45       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        93     93       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       177    177       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       181    181       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   221 AA;  24233 MW;  2F01B0B99CD7830D CRC64;
     MGDVSAPDGA SLPEKESAMT YTLPDLPYDY NALAPSISPE IMELHHDKHH AAYVKGANDA
     LEQLQAAREK GDLAAVNKLA KDLAFHLGGH INHSVFWKNM SPDGGGEPTG DVAEAIGEFF
     GSFDGFKKQF NAVANGIQGS GWSMLVWDTL GQRLNINQLF DQQGNLPVGQ LPILQLDMWE
     HAFYLQYKNV KGDYVNAWWD VVNWDDVAQR LAAAKAAGVS Y
//
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