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
//
