GenomeNet

Database: UniProt
Entry: A0A0F5N5Y2_9MYCO
LinkDB: A0A0F5N5Y2_9MYCO
Original site: A0A0F5N5Y2_9MYCO 
ID   A0A0F5N5Y2_9MYCO        Unreviewed;       207 AA.
AC   A0A0F5N5Y2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=AWC17_04760 {ECO:0000313|EMBL:ORW22639.1};
OS   Mycobacterium nebraskense.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=244292 {ECO:0000313|EMBL:ORW22639.1, ECO:0000313|Proteomes:UP000193781};
RN   [1] {ECO:0000313|EMBL:ORW22639.1, ECO:0000313|Proteomes:UP000193781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44803 {ECO:0000313|EMBL:ORW22639.1,
RC   ECO:0000313|Proteomes:UP000193781};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S.,
RA   Sara T., Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R.,
RA   Monica P., Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ORW22639.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LQPH01000120; ORW22639.1; -; Genomic_DNA.
DR   RefSeq; WP_046186039.1; NZ_LQPH01000120.1.
DR   EnsemblBacteria; KKC02474; KKC02474; WU83_24005.
DR   EnsemblBacteria; KLO33916; KLO33916; ABW17_27625.
DR   OrthoDB; 1440645at2; -.
DR   Proteomes; UP000193781; Unassembled WGS sequence.
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:UP000193781};
KW   Metal-binding {ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
SQ   SEQUENCE   207 AA;  22973 MW;  90B54B21459E1137 CRC64;
     MAEYTLPDLD WDYAALEPHI SGQINEIHHS KHHATYVKGV NDAVAKLEEA RANDDHAAIF
     LNEKNLAFHL GGHVNHSIWW KNLSPDGGDK PTGELGAAID DAFGSFDKFR AQFSAAANGL
     QGSGWAVLGY DTLGGRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWPDV QKRYAAATSK TSGLIFG
//
DBGET integrated database retrieval system