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}.
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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
//
