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Database: UniProt
Entry: F8GL10_NITSI
LinkDB: F8GL10_NITSI
Original site: F8GL10_NITSI 
ID   F8GL10_NITSI            Unreviewed;       213 AA.
AC   F8GL10;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   16-JAN-2019, entry version 35.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=Nit79A3_1988 {ECO:0000313|EMBL:AEJ01783.1};
OS   Nitrosomonas sp. (strain Is79A3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01783.1, ECO:0000313|Proteomes:UP000000501};
RN   [1] {ECO:0000313|EMBL:AEJ01783.1, ECO:0000313|Proteomes:UP000000501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01783.1,
RC   ECO:0000313|Proteomes:UP000000501};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A.,
RA   Norton J., Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D.,
RA   Woyke T.;
RT   "Complete sequence of Nitrosomonas sp. Is79A3.";
RL   Submitted (JUN-2011) 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; CP002876; AEJ01783.1; -; Genomic_DNA.
DR   RefSeq; WP_013966044.1; NC_015731.1.
DR   ProteinModelPortal; F8GL10; -.
DR   STRING; 261292.Nit79A3_1988; -.
DR   EnsemblBacteria; AEJ01783; AEJ01783; Nit79A3_1988.
DR   KEGG; nii:Nit79A3_1988; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; HNQFWEM; -.
DR   OrthoDB; 1440645at2; -.
DR   BioCyc; NSP261292:G1GYZ-1971-MONOMER; -.
DR   Proteomes; UP000000501; 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:UP000000501};
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:UP000000501}.
FT   DOMAIN       18    103       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      110    210       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        43     43       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        95     95       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       177    177       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       181    181       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   213 AA;  23372 MW;  B13CE0F572E3C148 CRC64;
     MSAVNLDNFS KAAQSGSQYV LAPLPYANNA LEPVITANTL SFHYGKHHKT YVDNLNNLLA
     NSDLAGQSLE QIIRATAGQA DKAAIFNNAA QVWNHMFYWH SLKPNGGGEP SAALKQKIEA
     SFGNLDACKK EFAQAALTQF GSGWAWLVLD GDKVAIAKTG NAETPLTKNV RPLLTIDVWE
     HAYYLDYQNR RADYVNTVLD KLINWDFAAA NLG
//
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