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Database: UniProt/TrEMBL
Entry: G8N286_GEOTH
LinkDB: G8N286_GEOTH
Original site: G8N286_GEOTH 
ID   G8N286_GEOTH            Unreviewed;       204 AA.
AC   G8N286;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   25-OCT-2017, entry version 33.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GTCCBUS3UF5_27730 {ECO:0000313|EMBL:AEV20076.1};
OS   Geobacillus thermoleovorans CCB_US3_UF5.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV20076.1, ECO:0000313|Proteomes:UP000005636};
RN   [1] {ECO:0000313|EMBL:AEV20076.1, ECO:0000313|Proteomes:UP000005636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV20076.1,
RC   ECO:0000313|Proteomes:UP000005636};
RA   Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT   "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT   CCB_US3_UF5.";
RL   Submitted (NOV-2011) 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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP003125; AEV20076.1; -; Genomic_DNA.
DR   RefSeq; WP_011231937.1; NC_016593.1.
DR   ProteinModelPortal; G8N286; -.
DR   SMR; G8N286; -.
DR   EnsemblBacteria; AEV20076; AEV20076; GTCCBUS3UF5_27730.
DR   GeneID; 32064341; -.
DR   KEGG; gte:GTCCBUS3UF5_27730; -.
DR   PATRIC; fig|1111068.3.peg.2685; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; GTHE1111068:GJY8-2837-MONOMER; -.
DR   Proteomes; UP000005636; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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:UP000005636};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        82     82       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   204 AA;  22890 MW;  8AE0B293B82D2C46 CRC64;
     MPFELPALPY PYDALEPHID KETMNIHHTK HHNTYVTNLN AALEGHPDLQ NKSLEELLSN
     LEALPESIRT AVRNNGGGHA NHSLFWTILS PNGGGEPTGE LAEAINKKFG SFTAFKDEFS
     KAAAGRFGSG WAWLVVNNGE LEITSTPNQD SPIMEGKTPI LGLDVWEHAY YLKYQNRRPE
     YIAAFWNIVN WDEVAKRYSE AKAK
//
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