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Database: UniProt
Entry: D5GMK9_TUBMM
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ID   D5GMK9_TUBMM            Unreviewed;       208 AA.
AC   D5GMK9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   16-JAN-2019, entry version 39.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GSTUM_00010782001 {ECO:0000313|EMBL:CAZ85752.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ85752.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ85752.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ85752.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M.,
RA   Jaillon O., Montanini B., Morin E., Noel B., Percudani R., Porcel B.,
RA   Rubini A., Amicucci A., Amselem J., Anthouard V., Arcioni S.,
RA   Artiguenave F., Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A.,
RA   Buee M., Cantarel B., Chevalier G., Couloux A., Da Silva C.,
RA   Denoeud F., Duplessis S., Ghignone S., Hilselberger B., Iotti M.,
RA   Marcais B., Mello A., Miranda M., Pacioni G., Quesneville H.,
RA   Riccioni C., Ruotolo R., Splivallo R., Stocchi V., Tisserant E.,
RA   Viscomi A.R., Zambonelli A., Zampieri E., Henrissat B., Lebrun M.H.,
RA   Paolocci F., Bonfante P., Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and
RT   mechanisms of symbiosis.";
RL   Nature 464:1033-1038(2010).
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}.
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DR   EMBL; FN430357; CAZ85752.1; -; Genomic_DNA.
DR   RefSeq; XP_002841561.1; XM_002841515.1.
DR   UniGene; Tme.980; -.
DR   ProteinModelPortal; D5GMK9; -.
DR   STRING; 39416.CAZ85752; -.
DR   EnsemblFungi; CAZ85752; CAZ85752; GSTUM_00010782001.
DR   GeneID; 9182178; -.
DR   KEGG; tml:GSTUM_00010782001; -.
DR   InParanoid; D5GMK9; -.
DR   KO; K04564; -.
DR   OMA; YEGWKGE; -.
DR   Proteomes; UP000006911; 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:UP000006911};
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:UP000006911}.
FT   DOMAIN        5     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       99    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        30     30       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        78     78       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       169    169       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  23110 MW;  CD81604B4DF6D18D CRC64;
     MAVANFTLPA LPYAYDALEP YISGQIMQIH HSKHHQTYVN NLNAATANHV KALQGNDVRA
     QINLQQAIKF NGGGHINHSL FWANLAPANT SQAKPESAEK LTEAISAKYG SYDGFKDEFM
     GVLLGLQGSG WGWLVKDKKT EQLDIVTTKD QDPVVGDLAP ILGIDMWEHA YYLQYFNDKA
     SYVNGIWNII NWETAEGRFL GRSGTLEL
//
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