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Database: UniProt/TrEMBL
Entry: A0A0E0TDU4_GEOS2
LinkDB: A0A0E0TDU4_GEOS2
Original site: A0A0E0TDU4_GEOS2 
ID   A0A0E0TDU4_GEOS2        Unreviewed;       204 AA.
AC   A0A0E0TDU4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=GYMC52_2492 {ECO:0000313|EMBL:ADU94873.1};
OS   Geobacillus sp. (strain Y412MC52).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=550542 {ECO:0000313|EMBL:ADU94873.1, ECO:0000313|Proteomes:UP000002223};
RN   [1] {ECO:0000313|EMBL:ADU94873.1, ECO:0000313|Proteomes:UP000002223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC52 {ECO:0000313|EMBL:ADU94873.1,
RC   ECO:0000313|Proteomes:UP000002223};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y412MC52.";
RL   Submitted (JAN-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; CP002442; ADU94873.1; -; Genomic_DNA.
DR   RefSeq; WP_011231937.1; NC_014915.1.
DR   ProteinModelPortal; A0A0E0TDU4; -.
DR   SMR; A0A0E0TDU4; -.
DR   EnsemblBacteria; ADU94873; ADU94873; GYMC52_2492.
DR   GeneID; 32064341; -.
DR   KEGG; gya:GYMC52_2492; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; GSP550542:GH52-2456-MONOMER; -.
DR   Proteomes; UP000002223; 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:UP000002223};
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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