ID W0ERB5_9BACT Unreviewed; 192 AA.
AC W0ERB5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 16-JAN-2019, entry version 22.
DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN ORFNames=BARVI_04015 {ECO:0000313|EMBL:AHF12098.1};
OS Barnesiella viscericola DSM 18177.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF12098.1, ECO:0000313|Proteomes:UP000018901};
RN [1] {ECO:0000313|EMBL:AHF12098.1, ECO:0000313|Proteomes:UP000018901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007034; AHF12098.1; -; Genomic_DNA.
DR RefSeq; WP_025277965.1; NZ_CP007034.1.
DR EnsemblBacteria; AHF12098; AHF12098; BARVI_04015.
DR KEGG; bvs:BARVI_04015; -.
DR PATRIC; fig|880074.11.peg.846; -.
DR KO; K04564; -.
DR OrthoDB; 1440645at2; -.
DR Proteomes; UP000018901; 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:UP000018901};
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:UP000018901}.
FT DOMAIN 3 79 Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT DOMAIN 89 190 Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT METAL 27 27 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 74 74 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 157 157 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
FT METAL 161 161 Divalent metal cation.
FT {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ SEQUENCE 192 AA; 22385 MW; F59F9225198F04FD CRC64;
MIYQLPPLPY GTNDLAPVIS QETIEYHYGK HEQTYLDNLN RLIDGTPYAE KPLEEVIREA
EGALFNNASQ AWNHIFYFFT FAPDGRRKPQ GKLAEAIDRQ WGSLENFQKE FEQAGVTLFG
SGWVWLSKDP EGKLVISQES NAGSPLKKGY TPLLTFDVWE HAYYIDYRNR RAEHLHRLWE
IVDWSVVEAR YL
//
