ID A0A0X8K3S2_9ACTO Unreviewed; 207 AA.
AC A0A0X8K3S2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 02-DEC-2020, entry version 16.
DE RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
GN ORFNames=AXE84_11840 {ECO:0000313|EMBL:AME00013.1};
OS Actinomyces oris.
OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; 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 -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC {ECO:0000256|ARBA:ARBA00002170}.
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|ARBA:ARBA00001605,
CC ECO:0000256|RuleBase:RU000414};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714, 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 OrthoDB; 1440645at2; -.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000349-1, ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}.
FT DOMAIN 4..84
FT /note="Sod_Fe_N"
FT /evidence="ECO:0000259|Pfam:PF00081"
FT DOMAIN 91..193
FT /note="Sod_Fe_C"
FT /evidence="ECO:0000259|Pfam:PF02777"
FT METAL 28
FT /note="Divalent metal cation"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT METAL 76
FT /note="Divalent metal cation"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT METAL 160
FT /note="Divalent metal cation"
FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT METAL 164
FT /note="Divalent metal cation"
FT /evidence="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
//
