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Database: UniProt
Entry: A0A1B1Z659_9BACI
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ID   A0A1B1Z659_9BACI        Unreviewed;       203 AA.
AC   A0A1B1Z659;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   13-FEB-2019, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ABE41_012925 {ECO:0000313|EMBL:ANX12914.1};
OS   Fictibacillus arsenicus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX12914.1, ECO:0000313|Proteomes:UP000077412};
RN   [1] {ECO:0000313|EMBL:ANX12914.1, ECO:0000313|Proteomes:UP000077412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-54 {ECO:0000313|EMBL:ANX12914.1,
RC   ECO:0000313|Proteomes:UP000077412};
RA   Zheng Z.;
RT   "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain
RT   with toxicity to nematodes and a potential arsenic-resistance
RT   activity.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP016761; ANX12914.1; -; Genomic_DNA.
DR   RefSeq; WP_066290962.1; NZ_CP016761.1.
DR   EnsemblBacteria; ANX12914; ANX12914; ABE41_012925.
DR   KEGG; far:ABE41_012925; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; GCF_001642935:G1ET8-2619-MONOMER; -.
DR   Proteomes; UP000077412; 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:UP000077412};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077412}.
FT   DOMAIN        3     90       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    198       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   203 AA;  22841 MW;  AE74B5470CDB34F9 CRC64;
     MAKFELPALP YESNALEPHI DKETMEIHHG RHHKTYVDNL NAALEGQSEF ENKSLEDILS
     NLDSLPQNIQ TAVRNNGGGH ANHSLFWEVI APGGANSPSG ELADKINSKF GSLEAFKEEF
     ANAGKTRFGS GWAWLVVNNG ELEVTSTPNQ DNPVMEGKTP ILGLDVWEHA YYLKYQNKRP
     DYIAAFWNVV NWDEVEKRYN EAK
//
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