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Database: UniProt/TrEMBL
Entry: A0A0X8K3S2_9ACTO
LinkDB: A0A0X8K3S2_9ACTO
Original site: A0A0X8K3S2_9ACTO 
ID   A0A0X8K3S2_9ACTO        Unreviewed;       207 AA.
AC   A0A0X8K3S2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AXE84_11840 {ECO:0000313|EMBL:AME00013.1};
OS   Actinomyces oris.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=544580 {ECO:0000313|EMBL:AME00013.1, ECO:0000313|Proteomes:UP000067270};
RN   [1] {ECO:0000313|EMBL:AME00013.1, ECO:0000313|Proteomes:UP000067270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T14V {ECO:0000313|EMBL:AME00013.1,
RC   ECO:0000313|Proteomes:UP000067270};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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; CP014232; AME00013.1; -; Genomic_DNA.
DR   RefSeq; WP_010615073.1; NZ_MAUB01000282.1.
DR   EnsemblBacteria; AME00013; AME00013; AXE84_11840.
DR   GeneID; 31655590; -.
DR   KEGG; aos:AXE84_11840; -.
DR   KO; K04564; -.
DR   Proteomes; UP000067270; 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:UP000067270};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
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;  22711 MW;  EB16DF9DF26E41C8 CRC64;
     MAVYTLPELP YDYAALEPHI SGKIMELHHD KHHAAYVAGA NAALEALSAA REAGDLAAIN
     LWEKNLAFNL GGHTNHSIFW KNLSPNGGGQ PEGELAEAIK DSFGSFEKFQ AQFTATAMGI
     QGSGWAVLAY DSLSGKLVTF QLFDQQGNVP VGTIPLFMVD MWEHAFYLDY LNVKADYVKA
     VWNIANWQDV SERLANAVAK AQDLIVR
//
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