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Database: UniProt
Entry: A0A0J6F0V2_9BACI
LinkDB: A0A0J6F0V2_9BACI
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ID   A0A0J6F0V2_9BACI        Unreviewed;       204 AA.
AC   A0A0J6F0V2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AB447_221575 {ECO:0000313|EMBL:KRT92875.1}, COP00_04080
GN   {ECO:0000313|EMBL:ATH91897.1};
OS   Bacillus glycinifermentans.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1664069 {ECO:0000313|EMBL:KRT92875.1, ECO:0000313|Proteomes:UP000036168};
RN   [1] {ECO:0000313|EMBL:KRT92875.1, ECO:0000313|Proteomes:UP000036168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GO-13 {ECO:0000313|EMBL:KRT92875.1,
RC   ECO:0000313|Proteomes:UP000036168};
RX   PubMed=26297378; DOI=10.1099/ijsem.0.000462;
RA   Kim S.J., Dunlap C.A., Kwon S.W., Rooney A.P.;
RT   "Bacillus glycinifermentans sp. nov., isolated from fermented soybean
RT   paste.";
RL   Int. J. Syst. Evol. Microbiol. 65:3586-3590(2015).
RN   [2] {ECO:0000313|EMBL:KRT92875.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GO-13 {ECO:0000313|EMBL:KRT92875.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ATH91897.1, ECO:0000313|Proteomes:UP000218414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBN06P03352 {ECO:0000313|EMBL:ATH91897.1,
RC   ECO:0000313|Proteomes:UP000218414};
RA   Yu W.-S., Do H.-N., Cheong H.-M., Hwang K.-J.;
RT   "Whole genome sequencing of Bacillus glycinfermentans NCCP 15922.";
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}.
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DR   EMBL; CP023481; ATH91897.1; -; Genomic_DNA.
DR   EMBL; LECW02000026; KRT92875.1; -; Genomic_DNA.
DR   RefSeq; WP_048405984.1; NZ_LECW02000026.1.
DR   EnsemblBacteria; KRT92875; KRT92875; AB447_221575.
DR   PATRIC; fig|1664069.3.peg.5277; -.
DR   Proteomes; UP000036168; Unassembled WGS sequence.
DR   Proteomes; UP000218414; Chromosome.
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:UP000036168,
KW   ECO:0000313|Proteomes:UP000218414};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        3     91       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        83     83       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   204 AA;  22626 MW;  633C5191CB2775B7 CRC64;
     MSKYELPALP YSFSALEPNI DEETMKIHHG RHHATYVNNL NAALEGRDEL AGKSVEDLIA
     NLDAVPDEIR TAVRNNGGGH ANHSLFWNIL SPNGGGAPAG EIAEAINQTF GSFDQFKEEF
     AKAAAGRFGS GWAWLVVDKD RLAITSTPNQ DSPLMEGQKP VLGLDVWEHA YYLKYQNKRP
     DYISAFFNVV NWEAVNQYYQ AARG
//
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