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Database: UniProt/TrEMBL
Entry: Q5Z3M8_NOCFA
LinkDB: Q5Z3M8_NOCFA
Original site: Q5Z3M8_NOCFA 
ID   Q5Z3M8_NOCFA            Unreviewed;       206 AA.
AC   Q5Z3M8;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   28-MAR-2018, entry version 90.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=sodF {ECO:0000313|EMBL:BAD54963.1};
GN   OrderedLocusNames=NFA_1210 {ECO:0000313|EMBL:BAD54963.1};
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD54963.1, ECO:0000313|Proteomes:UP000006820};
RN   [1] {ECO:0000313|EMBL:BAD54963.1, ECO:0000313|Proteomes:UP000006820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD54963.1,
RC   ECO:0000313|Proteomes:UP000006820};
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD54963.1; -; Genomic_DNA.
DR   RefSeq; WP_011206650.1; NC_006361.1.
DR   ProteinModelPortal; Q5Z3M8; -.
DR   STRING; 247156.nfa1210; -.
DR   EnsemblBacteria; BAD54963; BAD54963; NFA_1210.
DR   KEGG; nfa:NFA_1210; -.
DR   eggNOG; ENOG4105CK4; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; POG091H03Q7; -.
DR   Proteomes; UP000006820; 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:UP000006820};
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:UP000006820}.
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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