ID A0A0X8K3S2_9ACTO Unreviewed; 207 AA.
AC A0A0X8K3S2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 05-FEB-2025, entry version 32.
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=RMW62_06020 {ECO:0000313|EMBL:MDT0248639.1};
OS Actinomyces oris.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Actinomycetales;
OC Actinomycetaceae; Actinomyces.
OX NCBI_TaxID=544580 {ECO:0000313|EMBL:MDT0248639.1, ECO:0000313|Proteomes:UP001180729};
RN [1] {ECO:0000313|EMBL:MDT0248639.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNGBCC1803368 {ECO:0000313|EMBL:MDT0248639.1};
RA Ye Y., Liu C., Zhao J., Xu J., Huang H., Wang B., Wei J., Jing X.;
RT "Draft Genome Sequences of Three Actinomyces oris Strains, Isolated from
RT Healthy Human Feces.";
RL Submitted (JUN-2022) 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:
CC Reaction=2 superoxide + 2 H(+) = 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|RuleBase:RU000414};
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MDT0248639.1}.
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DR EMBL; JAMZMH010000005; MDT0248639.1; -; Genomic_DNA.
DR RefSeq; WP_010615073.1; NZ_MAUB01000282.1.
DR AlphaFoldDB; A0A0X8K3S2; -.
DR KEGG; aos:AXE84_11840; -.
DR Proteomes; UP001180729; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR FunFam; 1.10.287.990:FF:000001; Superoxide dismutase; 1.
DR FunFam; 3.55.40.20:FF:000004; Superoxide dismutase [Fe]; 1.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR InterPro; IPR050265; Fe/Mn_Superoxide_Dismutase.
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 PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
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; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000414};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000414}.
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
//
