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Database: UniProt
Entry: A0A0L0LFE0_9BACT
LinkDB: A0A0L0LFE0_9BACT
Original site: A0A0L0LFE0_9BACT 
ID   A0A0L0LFE0_9BACT        Unreviewed;       197 AA.
AC   A0A0L0LFE0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-MAR-2018, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AB198_00205 {ECO:0000313|EMBL:KND48729.1};
OS   Parcubacteria bacterium C7867-003.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1659197 {ECO:0000313|EMBL:KND48729.1, ECO:0000313|Proteomes:UP000036964};
RN   [1] {ECO:0000313|EMBL:KND48729.1, ECO:0000313|Proteomes:UP000036964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7867-003 {ECO:0000313|EMBL:KND48729.1};
RX   PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA   Nelson W.C., Stegen J.C.;
RT   "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT   symbiotic lifestyle.";
RL   Front. Microbiol. 6:713-713(2015).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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:KND48729.1}.
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DR   EMBL; LFCM01000026; KND48729.1; -; Genomic_DNA.
DR   EnsemblBacteria; KND48729; KND48729; AB198_00205.
DR   Proteomes; UP000036964; 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; 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   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000036964};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:KND48729.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036964}.
FT   DOMAIN       17     83       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    191       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        25     25       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        75     75       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       158    158       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   197 AA;  23028 MW;  399CAB8D20A079BF CRC64;
     MKPFEEKKFN IPELKGISAK TIEEHLKLYS GYVKNANLVG TKLGEMWTED KEKHMYAMSE
     LARRFSFEYN GMRNHEVYFD ILSDGTTPLS DGELKKAIEK SYGTVETFLE IFKAMAMTRG
     VGWAMVWYDK QEDRLINSWV DEQHLGQLQG CALILGLDMW EHSFVYDYQP SGKKQYVEDF
     FANLNWSKVE ENFNKAK
//
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