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Database: UniProt/TrEMBL
Entry: A0A178TZK7_GEOTM
LinkDB: A0A178TZK7_GEOTM
Original site: A0A178TZK7_GEOTM 
ID   A0A178TZK7_GEOTM        Unreviewed;       204 AA.
AC   A0A178TZK7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GT23_1605 {ECO:0000313|EMBL:OAO86587.1};
OS   Geobacillus thermoglucosidasius (Bacillus thermoglucosidasius).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Parageobacillus.
OX   NCBI_TaxID=1426 {ECO:0000313|EMBL:OAO86587.1, ECO:0000313|Proteomes:UP000078422};
RN   [1] {ECO:0000313|EMBL:OAO86587.1, ECO:0000313|Proteomes:UP000078422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GT23 {ECO:0000313|EMBL:OAO86587.1,
RC   ECO:0000313|Proteomes:UP000078422};
RA   Boekhorst J., Berendsen E.M., Wells-Bennik M.H., Kuipers O.P.;
RT   "Spore heat resistance.";
RL   Submitted (MAR-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: 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAO86587.1}.
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DR   EMBL; LUCT01000026; OAO86587.1; -; Genomic_DNA.
DR   RefSeq; WP_003249146.1; NZ_LUCT01000026.1.
DR   EnsemblBacteria; OAO86587; OAO86587; GT23_1605.
DR   GeneID; 29240122; -.
DR   KEGG; ptl:AOT13_16765; -.
DR   PATRIC; fig|1426.34.peg.1098; -.
DR   KO; K04564; -.
DR   Proteomes; UP000078422; 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   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   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:UP000078422};
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;  22953 MW;  20FC29B7AD95BE52 CRC64;
     MAFELPQLPY AYDALEPYID KETMNIHHTK HHNTYVTNLN AALEGHADLQ NKSLEELLSN
     LEALPESIRT AVRNNGGGHA NHSLFWTILS PNGGGEPTGE LAEAINKKFG SFAAFKEEFT
     KAATTRFGSG WAWLVVNNGE LEVTSTPNQD SPLMEGKTPI LGLDVWEHAY YLKYQNRRPE
     YIAAFWNIVN WDEVAKRYSE AKAK
//
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