GenomeNet

Database: UniProt/TrEMBL
Entry: A0A1U9PIF8_9MYCO
LinkDB: A0A1U9PIF8_9MYCO
Original site: A0A1U9PIF8_9MYCO 
ID   A0A1U9PIF8_9MYCO        Unreviewed;       205 AA.
AC   A0A1U9PIF8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-MAR-2018, entry version 6.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=B1R94_18590 {ECO:0000313|EMBL:AQT80844.1};
OS   Mycobacterium litorale.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=758802 {ECO:0000313|EMBL:AQT80844.1, ECO:0000313|Proteomes:UP000189653};
RN   [1] {ECO:0000313|EMBL:AQT80844.1, ECO:0000313|Proteomes:UP000189653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F4 {ECO:0000313|EMBL:AQT80844.1,
RC   ECO:0000313|Proteomes:UP000189653};
RA   Li Y., Luo F.;
RT   "The complete genome sequences of a quinolinic acid degrading
RT   bacterium, Mycobacterium sp. F4.";
RL   Submitted (FEB-2017) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP019882; AQT80844.1; -; Genomic_DNA.
DR   KEGG; mll:B1R94_18590; -.
DR   KO; K04564; -.
DR   Proteomes; UP000189653; 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:UP000189653};
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:UP000189653}.
FT   DOMAIN        4     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   205 AA;  22669 MW;  17D4D02FB47D5E7D CRC64;
     MTHYTLPDLD YDYGALEPHI SGQINEIHHS KHHATYVKGA NDAIAKLDEA RASGDHSAIL
     LNEKNLAFHL GGHVNHSIWW KNLSPNGGDK PTGELAAAID DQFGSFDAFA AQFAAAANGL
     QGSGWAVLGY DTLGRRLLTF QLYDQQANVP LAVIPLLQVD MWEHAYYLQY KNVKADYVTA
     FWNVVNWDDV QARFASARAA EGLIF
//
DBGET integrated database retrieval system