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Database: UniProt/TrEMBL
Entry: V5X599_MYCNE
LinkDB: V5X599_MYCNE
Original site: V5X599_MYCNE 
ID   V5X599_MYCNE            Unreviewed;       207 AA.
AC   V5X599;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   25-OCT-2017, entry version 22.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=D174_00590 {ECO:0000313|EMBL:AHC23177.1};
OS   Mycobacterium neoaurum VKM Ac-1815D.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC23177.1, ECO:0000313|Proteomes:UP000018763};
RN   [1] {ECO:0000313|EMBL:AHC23177.1, ECO:0000313|Proteomes:UP000018763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC23177.1};
RX   PubMed=24435872;
RA   Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A.,
RA   Schelkunov M.I., Strizhov N., Ivashina T.V., Ashapkin V.V.,
RA   Donova M.V.;
RT   "Complete Genome Sequence of Sterol-Transforming Mycobacterium
RT   neoaurum Strain VKM Ac-1815D.";
RL   Genome Announc. 2:e01177-13(2014).
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; CP006936; AHC23177.1; -; Genomic_DNA.
DR   RefSeq; WP_023985010.1; NC_023036.2.
DR   EnsemblBacteria; AHC23177; AHC23177; D174_00590.
DR   KEGG; mne:D174_00590; -.
DR   KO; K04564; -.
DR   Proteomes; UP000018763; Chromosome.
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:UP000018763};
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:UP000018763}.
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;  23070 MW;  847CBFD378F91F8A CRC64;
     MAEYTLPDLD YDYGALEPHI SGQINELHHS KHHATYVKGV NDAVAKLEEA RANDDQSAIF
     LNEKNLAFHL GGHVNHSIWW KNLSPNGGDK PEGDLAAAID DQFGSFDKFR AQFTAAANGL
     QGSGWAVLGY DSLGQRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWADV QDRYAKATAK TGGLIFG
//
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