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Database: UniProt/TrEMBL
Entry: A0A0M3RJG3_9ACTO
LinkDB: A0A0M3RJG3_9ACTO
Original site: A0A0M3RJG3_9ACTO 
ID   A0A0M3RJG3_9ACTO        Unreviewed;       207 AA.
AC   A0A0M3RJG3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AM609_05505 {ECO:0000313|EMBL:ALC99066.1};
OS   Actinomyces sp. oral taxon 414.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=712122 {ECO:0000313|EMBL:ALC99066.1, ECO:0000313|Proteomes:UP000061022};
RN   [1] {ECO:0000313|EMBL:ALC99066.1, ECO:0000313|Proteomes:UP000061022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0588 {ECO:0000313|EMBL:ALC99066.1,
RC   ECO:0000313|Proteomes:UP000061022};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-2015) 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; CP012590; ALC99066.1; -; Genomic_DNA.
DR   RefSeq; WP_053586462.1; NZ_CP012590.1.
DR   EnsemblBacteria; ALC99066; ALC99066; AM609_05505.
DR   KEGG; acq:AM609_05505; -.
DR   PATRIC; fig|712122.3.peg.1255; -.
DR   KO; K04564; -.
DR   Proteomes; UP000061022; 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:UP000061022};
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:UP000061022}.
FT   DOMAIN        4     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       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   207 AA;  22694 MW;  A82FEE4C5942E992 CRC64;
     MSVYTLPELP YDYAALEPHI SGRIMELHHD RHHAAYVTGA NAALEKLQAA REAGDHAAIN
     LHEKNLAFNL GGHINHSIFW KNLSPNGGGE PEGDLAEAIK DSFGSFEAFK AQFTAAALGI
     QGSGWAVLAY DSVSGRLVTF QMFDQQGNVP VGTIPLFQVD MWEHAFYLDY LNVKADYVKA
     VWNIANWQDA GERLAAATSR TPGLIVR
//
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