GenomeNet

Database: UniProt
Entry: A0A0G9HEY1_9GAMM
LinkDB: A0A0G9HEY1_9GAMM
Original site: A0A0G9HEY1_9GAMM 
ID   A0A0G9HEY1_9GAMM        Unreviewed;       192 AA.
AC   A0A0G9HEY1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   13-FEB-2019, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=BJI69_13175 {ECO:0000313|EMBL:APG04753.1};
OS   Luteibacter rhizovicinus DSM 16549.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG04753.1, ECO:0000313|Proteomes:UP000182987};
RN   [1] {ECO:0000313|EMBL:APG04753.1, ECO:0000313|Proteomes:UP000182987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LJ96T {ECO:0000313|EMBL:APG04753.1,
RC   ECO:0000313|Proteomes:UP000182987};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP017480; APG04753.1; -; Genomic_DNA.
DR   RefSeq; WP_046966423.1; NZ_JPLB01000013.1.
DR   EnsemblBacteria; KLD68243; KLD68243; Y883_03910.
DR   KEGG; lrz:BJI69_13175; -.
DR   PATRIC; fig|1440763.5.peg.441; -.
DR   KO; K04564; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; GCF_001887595:G1FER-2644-MONOMER; -.
DR   Proteomes; UP000182987; 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:UP000182987};
KW   Metal-binding {ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
SQ   SEQUENCE   192 AA;  21338 MW;  2961C32E96E4FDDD CRC64;
     MAIELPPLPY EKNALEPHIS AETLEFHYGK HHQTYVTNLN NLIKGTEFEG KDLVDIVKAS
     SGGIFNNAAQ VWNHTFYWNS MRAPGGAEPP AKLADALTKA FGGVDKFKEE FAKSAAGNFG
     SGWTWLVQRP DGSLAIVNTS NAATPITGSD KPLFTADVWE HAYYIDYRNA RPKYLEAFWN
     LVNWDFAAKN LA
//
DBGET integrated database retrieval system