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Database: UniProt
Entry: A0A1W6L9R4_9BURK
LinkDB: A0A1W6L9R4_9BURK
Original site: A0A1W6L9R4_9BURK 
ID   A0A1W6L9R4_9BURK        Unreviewed;       193 AA.
AC   A0A1W6L9R4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   05-DEC-2018, entry version 9.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=A4W93_14130 {ECO:0000313|EMBL:ARN20944.1};
OS   Rhizobacter gummiphilus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Rhizobacter.
OX   NCBI_TaxID=946333 {ECO:0000313|EMBL:ARN20944.1, ECO:0000313|Proteomes:UP000193427};
RN   [1] {ECO:0000313|EMBL:ARN20944.1, ECO:0000313|Proteomes:UP000193427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS21 {ECO:0000313|EMBL:ARN20944.1,
RC   ECO:0000313|Proteomes:UP000193427};
RA   Tabata M., Kasai D., Fukuda M.;
RT   "Complete genome sequence of natural rubber-degrading, novel Gram-
RT   negative bacterium, Rhizobacter gummiphilus strain NS21.";
RL   Submitted (APR-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; CP015118; ARN20944.1; -; Genomic_DNA.
DR   KEGG; rgu:A4W93_14130; -.
DR   KO; K04564; -.
DR   Proteomes; UP000193427; 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:UP000193427};
KW   Metal-binding {ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193427}.
SQ   SEQUENCE   193 AA;  21376 MW;  2460C28B6FCCC60D CRC64;
     MEHTLPALPY AQDALAPHLS KETLEYHYGK HHNAYVVNLN NLQKGTEFEN LSLEDIIKKS
     SGGIYNNAAQ IWNHTFFWNS MKPNGGGEPK GALAAAIEAK FGSFAAFKEA FTKSAVGNFG
     SGWTWLVKKP DGSVDIVNTG AAGTPLTTAD KALLTIDVWE HAYYIDYRNL RPKFVETFLT
     SLANWDFAEK NFA
//
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