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Database: UniProt
Entry: A0A1G9VRP6_9ACTO
LinkDB: A0A1G9VRP6_9ACTO
Original site: A0A1G9VRP6_9ACTO 
ID   A0A1G9VRP6_9ACTO        Unreviewed;       213 AA.
AC   A0A1G9VRP6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   05-DEC-2018, entry version 5.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SAMN04487766_106108 {ECO:0000313|EMBL:SDM74661.1},
GN   SAMN05216355_11234 {ECO:0000313|EMBL:SDN74014.1};
OS   Actinomyces ruminicola.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=332524 {ECO:0000313|EMBL:SDM74661.1, ECO:0000313|Proteomes:UP000199671};
RN   [1] {ECO:0000313|EMBL:SDM74661.1, ECO:0000313|Proteomes:UP000198541, ECO:0000313|Proteomes:UP000199671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27982 {ECO:0000313|EMBL:SDN74014.1,
RC   ECO:0000313|Proteomes:UP000198541}, and KPR-7B
RC   {ECO:0000313|EMBL:SDM74661.1, ECO:0000313|Proteomes:UP000199671};
RA   de Groot N.N.;
RL   Submitted (OCT-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:
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|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; FNHU01000006; SDM74661.1; -; Genomic_DNA.
DR   EMBL; FNIM01000012; SDN74014.1; -; Genomic_DNA.
DR   Proteomes; UP000198541; Unassembled WGS sequence.
DR   Proteomes; UP000199671; 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   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:UP000198541,
KW   ECO:0000313|Proteomes:UP000199671};
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:UP000199671}.
FT   DOMAIN        9     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    199       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        34     34       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       170    170       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   213 AA;  23317 MW;  21E0CB802280C091 CRC64;
     MTTPTDTAKY TLPELPYDYA ALEPHISGRI MELHHDRHHA AYVTGANAAL EQLAAARAEG
     DFAAINLWEK NLAFNLGGHL NHSIFWKNLS PSGGGEPEGE LAEAIKDSFG SFAALKQQLN
     AAALGIQGSG WAVLAYDSVS GRLVTFQLFD QQGNVPVGTI PLFQIDMWEH AFYLDYLNVK
     ADYLAAIWQI VNWEDVAERL ANAVAHAEGL IVR
//
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