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Database: UniProt
Entry: A0A0A8EWB3_9ACTN
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ID   A0A0A8EWB3_9ACTN        Unreviewed;       213 AA.
AC   A0A0A8EWB3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   05-DEC-2018, entry version 18.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GZL_05776 {ECO:0000313|EMBL:AJC58351.1};
OS   Streptomyces sp. 769.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC58351.1, ECO:0000313|Proteomes:UP000031113};
RN   [1] {ECO:0000313|EMBL:AJC58351.1, ECO:0000313|Proteomes:UP000031113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=769 {ECO:0000313|EMBL:AJC58351.1,
RC   ECO:0000313|Proteomes:UP000031113};
RA   Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT   "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL   Submitted (DEC-2012) 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; CP003987; AJC58351.1; -; Genomic_DNA.
DR   RefSeq; WP_039636382.1; NZ_CP003987.1.
DR   EnsemblBacteria; AJC58351; AJC58351; GZL_05776.
DR   KEGG; stre:GZL_05776; -.
DR   KO; K04564; -.
DR   Proteomes; UP000031113; 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:UP000031113};
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:UP000031113}.
FT   DOMAIN        3     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    198       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       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   213 AA;  23509 MW;  7B512FFC1297023C CRC64;
     MATYTLPELP YDYSALAPVI SPEIIELHHD KHHAAYVKGA NDTLEQLAEA RDKDQWGSIN
     GLQKNLAFHL SGHILHSIYW HNMTGDGGGE PLEADGVGEL ADALAESFGS FAKFKAQLTK
     ASATTQGSGW GVLAYEPVTG RLIVEQVYDH QGNVGQGSVP ILVFDAWEHA FYLQYKNQKV
     DFIEAMWQVV NWQDVAKRYA AAKERADSLL LAP
//
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