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SODM_DEBHA
ID   SODM_DEBHA              Reviewed;         211 AA.
AC   Q6BQZ1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3};
DE   Flags: Precursor;
GN   OrderedLocusNames=DEHA2E01232g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological systems.
CC       {ECO:0000250|UniProtKB:P04179}.
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:0000250|UniProtKB:P0A0J3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q9UQX0};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9UQX0};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P04179}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9UQX0}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382137; CAG87585.1; -; Genomic_DNA.
DR   RefSeq; XP_459379.1; XM_459379.1.
DR   AlphaFoldDB; Q6BQZ1; -.
DR   SMR; Q6BQZ1; -.
DR   STRING; 4959.XP_459379.1; -.
DR   EnsemblFungi; CAG87585; CAG87585; DEHA2E01232g.
DR   GeneID; 2902917; -.
DR   KEGG; dha:DEHA2E01232g; -.
DR   VEuPathDB; FungiDB:DEHA2E01232g; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   HOGENOM; CLU_031625_2_1_1; -.
DR   InParanoid; Q6BQZ1; -.
DR   OMA; LNNWWNV; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; 3.55.40.20; -; 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   Antioxidant; Manganese; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..211
FT                   /note="Probable superoxide dismutase [Mn], mitochondrial"
FT                   /id="PRO_0000032884"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         84
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
FT   BINDING         177
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:P04179"
SQ   SEQUENCE   211 AA;  23719 MW;  F8BD6CDFA3DA149C CRC64;
     MSNSPAFGKN KIELPQLDWA YDSLEPYISG KINEIHHKKH HQTYVNGYNS AIEQLIEAES
     QGDVKKAIVI QQNIKFHGGG HTNHVLFWKS LAPNSQNGGK HPGSDTNLGK KIIEQYGSID
     NLISITNAKL ASIQGSGWAF IVKNKQNGGN LDVVTTYNQD TVTDPLVPLI AIDAWEHAYY
     LQYQNVKADY FKAIWNVINW EEASKRFDSH L
 
 
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