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Database: UniProt
Entry: T0R8E6_9PROT
LinkDB: T0R8E6_9PROT
Original site: T0R8E6_9PROT 
ID   T0R8E6_9PROT            Unreviewed;       191 AA.
AC   T0R8E6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, 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   Name=sodB {ECO:0000313|EMBL:EQC46664.1};
GN   ORFNames=M900_2428 {ECO:0000313|EMBL:EQC46664.1};
OS   Bacteriovorax sp. Seq25_V.
OC   Bacteria; Proteobacteria; Oligoflexia; Bacteriovoracales;
OC   Bacteriovoracaceae; Bacteriovorax.
OX   NCBI_TaxID=1201288 {ECO:0000313|EMBL:EQC46664.1};
RN   [1] {ECO:0000313|EMBL:EQC46664.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Seq25_V {ECO:0000313|EMBL:EQC46664.1};
RA   Chen H., Brinkac L.M., Mishra P., Dickerson T., Gordon-Bradley N.,
RA   Lymperopoulou D.S., Williams H.N., Badger J.H.;
RT   "Draft Genome Sequences for the obligate bacterial predators
RT   Bacteriovorax spp. of four phylogenetic clusters.";
RL   Submitted (JUL-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}.
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:EQC46664.1}.
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DR   EMBL; AUNI01000011; EQC46664.1; -; Genomic_DNA.
DR   RefSeq; WP_021273927.1; NZ_AUNI01000011.1.
DR   EnsemblBacteria; EQC46664; EQC46664; M900_2428.
DR   PATRIC; fig|1201288.3.peg.1080; -.
DR   OrthoDB; 1440645at2; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:EQC46664.1}.
FT   DOMAIN        2     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    189       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   191 AA;  21483 MW;  4BFC091E62132674 CRC64;
     MEHKLPELPW SKDALMPHIS PETIDYHYGK HHNAYVTNLN GLIKGTEFEN LSLEEIIMKS
     NGGLFNNAAQ VWNHTFYWNC LAPNAGGDAT GAVADKINAK WGSFEKFKEE FTKSAATNFG
     SGWTWLVKTA SGDLEIVNTS NAATPMTDGK TALLTVDVWE HAYYVDYRNA RPNYLTAFWS
     LVNWNFVNSN L
//
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