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Database: UniProt
Entry: A0A0M0EXP3_9BACI
LinkDB: A0A0M0EXP3_9BACI
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ID   A0A0M0EXP3_9BACI        Unreviewed;       202 AA.
AC   A0A0M0EXP3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-DEC-2018, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AKG34_15860 {ECO:0000313|EMBL:KON70080.1}, CN689_16910
GN   {ECO:0000313|EMBL:PEJ30980.1};
OS   Bacillus butanolivorans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=421767 {ECO:0000313|EMBL:KON70080.1, ECO:0000313|Proteomes:UP000037522};
RN   [1] {ECO:0000313|Proteomes:UP000037522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18926 {ECO:0000313|Proteomes:UP000037522};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Fjat-14236 dsm 18926.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KON70080.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 18926 {ECO:0000313|EMBL:KON70080.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PEJ30980.1, ECO:0000313|Proteomes:UP000220106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS003229 {ECO:0000313|EMBL:PEJ30980.1,
RC   ECO:0000313|Proteomes:UP000220106};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers
RT   conserved roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) 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:KON70080.1}.
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DR   EMBL; LGYA01000001; KON70080.1; -; Genomic_DNA.
DR   EMBL; NUEQ01000032; PEJ30980.1; -; Genomic_DNA.
DR   RefSeq; WP_053346971.1; NZ_NUEQ01000032.1.
DR   EnsemblBacteria; KON70080; KON70080; AKG34_15860.
DR   PATRIC; fig|421767.3.peg.4815; -.
DR   Proteomes; UP000037522; Unassembled WGS sequence.
DR   Proteomes; UP000220106; 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:UP000037522,
KW   ECO:0000313|Proteomes:UP000220106};
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   202 AA;  22591 MW;  7DBEAEC843DD66E1 CRC64;
     MAFELPQLPY AYDALEPHID KETMNIHHTK HHNTYVTNLN NALEGNQELL SKSVEEIVAN
     LDAVPEAVRT AVRNNGGGHA NHSLFWEILS PNGGGQPTGE LADAITSKFG SFDSFKEEFA
     KAATTRFGSG WAWLAVNNGE LEVTSTPNQD NPLSEGKTPL LGLDVWEHAY YLNYQNRRPE
     YINSFWNVVN WDEVAKRYSA AK
//
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