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Database: UniProt/TrEMBL
Entry: K0EMC4_9NOCA
LinkDB: K0EMC4_9NOCA
Original site: K0EMC4_9NOCA 
ID   K0EMC4_9NOCA            Unreviewed;       207 AA.
AC   K0EMC4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   28-MAR-2018, entry version 32.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=O3I_000385 {ECO:0000313|EMBL:AFT98039.1};
OS   Nocardia brasiliensis ATCC 700358.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=1133849 {ECO:0000313|EMBL:AFT98039.1, ECO:0000313|Proteomes:UP000006304};
RN   [1] {ECO:0000313|EMBL:AFT98039.1, ECO:0000313|Proteomes:UP000006304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HUJEG-1 {ECO:0000313|EMBL:AFT98039.1};
RX   PubMed=22535940; DOI=10.1128/JB.00210-12;
RA   Vera-Cabrera L., Ortiz-Lopez R., Elizondo-Gonzalez R.,
RA   Perez-Maya A.A., Ocampo-Candiani J.;
RT   "Complete genome sequence of Nocardia brasiliensis HUJEG-1.";
RL   J. Bacteriol. 194:2761-2762(2012).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; CP003876; AFT98039.1; -; Genomic_DNA.
DR   RefSeq; WP_014980904.1; NC_018681.1.
DR   ProteinModelPortal; K0EMC4; -.
DR   EnsemblBacteria; AFT98039; AFT98039; O3I_000385.
DR   KEGG; nbr:O3I_000385; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000006304; 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:UP000006304};
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:UP000006304}.
FT   DOMAIN        3     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       91    193       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        76     76       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   207 AA;  23074 MW;  2DFA901839E7CD0C CRC64;
     MAEYTLPDLD YDYSALEPHI SGQINELHHS KHHAAYVAGA NTALEKLEAA RESGDHGAIF
     LYEKNLAFHL GGHVNHSIWW KNLSPNGGDK PVGELAAAID DQFGSFDKFR GQFTAAANGL
     QGSGWAVLGY DTLGQKLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVTA
     FWNVVNWEDV QERFARAVSQ GKGLFFG
//
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