ID A0A0X8K3S2_9ACTO Unreviewed; 207 AA.
AC A0A0X8K3S2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 28-MAR-2018, entry version 11.
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 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 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
//
