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Database: UniProt
Entry: A0A150MMR9_9BACI
LinkDB: A0A150MMR9_9BACI
Original site: A0A150MMR9_9BACI 
ID   A0A150MMR9_9BACI        Unreviewed;       204 AA.
AC   A0A150MMR9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-DEC-2018, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=B4110_2585 {ECO:0000313|EMBL:KYD25764.1};
OS   Parageobacillus toebii.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Parageobacillus.
OX   NCBI_TaxID=153151 {ECO:0000313|EMBL:KYD25764.1, ECO:0000313|Proteomes:UP000075324};
RN   [1] {ECO:0000313|EMBL:KYD25764.1, ECO:0000313|Proteomes:UP000075324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4110 {ECO:0000313|EMBL:KYD25764.1,
RC   ECO:0000313|Proteomes:UP000075324};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A.,
RA   Holsappel S., Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated
RT   from Foods.";
RL   Submitted (JAN-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}.
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:KYD25764.1}.
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DR   EMBL; LQYW01000132; KYD25764.1; -; Genomic_DNA.
DR   RefSeq; WP_015864503.1; NZ_QREZ01000126.1.
DR   EnsemblBacteria; KYD25764; KYD25764; B4110_2585.
DR   PATRIC; fig|153151.4.peg.986; -.
DR   Proteomes; UP000075324; 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   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:UP000075324};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:KYD25764.1}.
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;  22911 MW;  45A462EDACDF49A4 CRC64;
     MAFELPQLPY AYDALEPHID KETMNIHHTK HHNTYVTNLN AALEGHADLQ NKSIEELLSN
     LEALPESIRT AVRNNGGGHA NHSLFWTILS PNGGGEPTGE LADAINKKFG SFAAFKEEFT
     KAAATRFGSG WAWLVVNNGE LEVTSTPNQD SPLMEGKTPI LGLDVWEHAY YLKYQNRRPE
     YIAAFWNIVN WDEVARRYSE AKAK
//
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