ID A0A1H1WS74_9ACTN Unreviewed; 208 AA.
AC A0A1H1WS74;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-FEB-2019, entry version 9.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=SAMN04489812_3778 {ECO:0000313|EMBL:SDS99882.1},
GN SAMN04489812_6147 {ECO:0000313|EMBL:SDT48207.1};
OS Microlunatus soli.
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Microlunatus.
OX NCBI_TaxID=630515 {ECO:0000313|EMBL:SDS99882.1, ECO:0000313|Proteomes:UP000199103};
RN [1] {ECO:0000313|EMBL:SDS99882.1, ECO:0000313|Proteomes:UP000199103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21800 {ECO:0000313|EMBL:SDS99882.1,
RC ECO:0000313|Proteomes:UP000199103};
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; LT629772; SDS99882.1; -; Genomic_DNA.
DR EMBL; LT629772; SDT48207.1; -; Genomic_DNA.
DR BioCyc; GCF_900105385:BLU38_RS18815-MONOMER; -.
DR BioCyc; GCF_900105385:BLU38_RS30645-MONOMER; -.
DR Proteomes; UP000199103; Chromosome i.
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:UP000199103};
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:UP000199103}.
FT DOMAIN 3 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 208 AA; 23221 MW; B6134BC4ED1E8C57 CRC64;
MAAYELPDLP YDYGALEPHI SGKIMELHHD KHHATYVKAV NTALDQLAEA RDKNSLGTVA
GLEKALAFNL GGHVNHSVFW PNLSPDGGDK PTGELGQAID EFFGSFDGFR AHFEATATTI
MGSGWAILAW DSLGQRLNIV QLYDQQGNLP IAQVPIVLLD MWEHAFYLDY QNVKPDYVKA
WWNVVNWADA QERFTRATQQ TKGLIIPN
//
