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Database: UniProt/TrEMBL
Entry: A0A0A1FVX4_9MYCO
LinkDB: A0A0A1FVX4_9MYCO
Original site: A0A0A1FVX4_9MYCO 
ID   A0A0A1FVX4_9MYCO        Unreviewed;       207 AA.
AC   A0A0A1FVX4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=G155_28790 {ECO:0000313|EMBL:AIY48848.1};
OS   Mycobacterium sp. VKM Ac-1817D.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1273687 {ECO:0000313|EMBL:AIY48848.1, ECO:0000313|Proteomes:UP000030340};
RN   [1] {ECO:0000313|EMBL:AIY48848.1, ECO:0000313|Proteomes:UP000030340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1817D {ECO:0000313|EMBL:AIY48848.1,
RC   ECO:0000313|Proteomes:UP000030340};
RX   PubMed=23474435; DOI=10.1016/j.jsbmb.2013.02.016;
RA   Bragin E.Y., Shtratnikova V.Y., Dovbnya D.V., Schelkunov M.I.,
RA   Pekov Y.A., Malakho S.G., Egorova O.V., Ivashina T.V., Sokolov S.L.,
RA   Ashapkin V.V., Donova M.V.;
RT   "Comparative analysis of genes encoding key steroid core oxidation
RT   enzymes in fast-growing Mycobacterium spp. strains.";
RL   J. Steroid Biochem. Mol. Biol. 138:41-53(2013).
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; CP009914; AIY48848.1; -; Genomic_DNA.
DR   RefSeq; WP_003883955.1; NZ_CP009914.1.
DR   SMR; A0A0A1FVX4; -.
DR   EnsemblBacteria; AIY48848; AIY48848; G155_28790.
DR   GeneID; 29424468; -.
DR   KEGG; myv:G155_28790; -.
DR   KO; K04564; -.
DR   Proteomes; UP000030340; 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:UP000030340};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:AIY48848.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030340}.
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;  22965 MW;  6B1A6B2EA57C82A1 CRC64;
     MAEYTLPDLD YDYGALEPHI SGQINELHHS KHHAAYVKGV NDAVAKLDEA RANGDHAAIF
     LNEKNLAFHL GGHVNHSIWW KNLSPNGGDK PTGDLAAAID DQFGSFDKFQ AQFTAAANGL
     QGSGWAVLGY DSLGDRLLTF QLYDQQANVP LGIIPLLQVD MWEHAFYLQY KNVKADYVKA
     FWNVVNWEDV QNRYAAATSK TNGLIFG
//
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