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Database: UniProt/TrEMBL
Entry: A0A0H5P0T3_NOCFR
LinkDB: A0A0H5P0T3_NOCFR
Original site: A0A0H5P0T3_NOCFR 
ID   A0A0H5P0T3_NOCFR        Unreviewed;       206 AA.
AC   A0A0H5P0T3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodA {ECO:0000313|EMBL:CRY80939.1};
GN   ORFNames=ERS450000_04120 {ECO:0000313|EMBL:CRY80939.1};
OS   Nocardia farcinica.
OG   Plasmid 2 {ECO:0000313|EMBL:CRY80939.1}.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=37329 {ECO:0000313|EMBL:CRY80939.1, ECO:0000313|Proteomes:UP000057820};
RN   [1] {ECO:0000313|EMBL:CRY80939.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC11134 {ECO:0000313|EMBL:CRY80939.1};
RC   PLASMID=2 {ECO:0000313|EMBL:CRY80939.1};
RA   Informatics Pathogen;
RL   Submitted (MAR-2015) 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: 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; LN868939; CRY80939.1; -; Genomic_DNA.
DR   RefSeq; WP_011206650.1; NZ_LN868939.1.
DR   ProteinModelPortal; A0A0H5P0T3; -.
DR   EnsemblBacteria; CRY80939; CRY80939; ERS450000_04120.
DR   KEGG; nfr:ERS450000_04120; -.
DR   KO; K04564; -.
DR   Proteomes; UP000057820; Plasmid 2.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
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:UP000057820};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CRY80939.1}; Plasmid {ECO:0000313|EMBL:CRY80939.1}.
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   206 AA;  22995 MW;  DC3BE10A913B109D CRC64;
     MAEYTLPDLD YDYSALEPHI SGQINELHHS KHHAAYVAGA NQALEKLEAA RESGDHSAIF
     LYEKNLAFHL GGHVNHSIWW KNLSPNGGDK PVGELAAAID DQFGSFDKFR AQFTAAANGL
     QGSGWAVLGY DTLGQKLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVTA
     FWNVVNWADV QDRFARAVNQ GKGLVF
//
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