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Database: UniProt
Entry: P00447
LinkDB: P00447
Original site: P00447 
ID   SODM_YEAST              Reviewed;         233 AA.
AC   P00447; D3DKV3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-1986, sequence version 1.
DT   13-FEB-2019, entry version 190.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SOD2; OrderedLocusNames=YHR008C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3882422; DOI=10.1111/j.1432-1033.1985.tb08731.x;
RA   Marres C.A.M., van Loon A.P.G.M., Oudshoorn P., van Steeg H.,
RA   Grivell L.A., Slater E.C.;
RT   "Nucleotide sequence analysis of the nuclear gene coding for manganese
RT   superoxide dismutase of yeast mitochondria, a gene previously assumed
RT   to code for the Rieske iron-sulphur protein.";
RL   Eur. J. Biochem. 147:153-161(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA   Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA   Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA   Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA   Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA   Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA   Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX   PubMed=3072251; DOI=10.1016/0378-1119(88)90318-6;
RA   Schrank I.S., Sims P.F., Oliver S.G.;
RT   "Functional expression of the yeast Mn-superoxide dismutase gene in
RT   Escherichia coli requires deletion of the signal peptide sequence.";
RL   Gene 73:121-130(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 27-233.
RA   Ditlow C., Johansen J.T., Martin B.M., Svendsen I.;
RT   "The complete amino acid sequence of manganese-superoxide dismutase
RT   from Saccharomyces cerevisae.";
RL   Carlsberg Res. Commun. 47:81-91(1982).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND THR-149, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.M700098-MCP200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: Present with 10900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; X02156; CAA26092.1; -; Genomic_DNA.
DR   EMBL; U10400; AAB68939.1; -; Genomic_DNA.
DR   EMBL; M24079; AAA35065.1; -; Genomic_DNA.
DR   EMBL; AY557821; AAS56147.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06697.1; -; Genomic_DNA.
DR   PIR; A00521; DSBYN.
DR   RefSeq; NP_011872.1; NM_001179138.1.
DR   PDB; 3BFR; X-ray; 2.05 A; A=27-233.
DR   PDB; 3LSU; X-ray; 1.90 A; A/B/C/D=27-233.
DR   PDB; 3RN4; X-ray; 1.79 A; A=19-233.
DR   PDB; 4E4E; X-ray; 1.88 A; A/B/C/D=27-233.
DR   PDB; 4F6E; X-ray; 1.60 A; A/B/C/D=28-233.
DR   PDBsum; 3BFR; -.
DR   PDBsum; 3LSU; -.
DR   PDBsum; 3RN4; -.
DR   PDBsum; 4E4E; -.
DR   PDBsum; 4F6E; -.
DR   ProteinModelPortal; P00447; -.
DR   SMR; P00447; -.
DR   BioGrid; 36435; 231.
DR   DIP; DIP-4905N; -.
DR   IntAct; P00447; 10.
DR   MINT; P00447; -.
DR   STRING; 4932.YHR008C; -.
DR   Allergome; 867; Sac c MnSOD.
DR   iPTMnet; P00447; -.
DR   UCD-2DPAGE; P00447; -.
DR   MaxQB; P00447; -.
DR   PaxDb; P00447; -.
DR   PRIDE; P00447; -.
DR   TopDownProteomics; P00447; -.
DR   EnsemblFungi; YHR008C_mRNA; YHR008C_mRNA; YHR008C.
DR   GeneID; 856399; -.
DR   KEGG; sce:YHR008C; -.
DR   EuPathDB; FungiDB:YHR008C; -.
DR   SGD; S000001050; SOD2.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; P00447; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   BioCyc; YEAST:MONOMER3O-1642; -.
DR   Reactome; R-SCE-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
DR   EvolutionaryTrace; P00447; -.
DR   PRO; PR:P00447; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:SGD.
DR   GO; GO:0001324; P:age-dependent response to oxidative stress involved in chronological cell aging; IMP:SGD.
DR   GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; IMP:SGD.
DR   GO; GO:0007568; P:aging; IBA:GO_Central.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:SGD.
DR   GO; GO:0001302; P:replicative cell aging; IMP:SGD.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing; Manganese;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     26       Mitochondrion. {ECO:0000269|Ref.6}.
FT   CHAIN        27    233       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032888.
FT   METAL        52     52       Manganese. {ECO:0000250}.
FT   METAL       107    107       Manganese. {ECO:0000250}.
FT   METAL       194    194       Manganese. {ECO:0000250}.
FT   METAL       198    198       Manganese. {ECO:0000250}.
FT   MOD_RES     147    147       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17761666}.
FT   MOD_RES     149    149       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17761666}.
FT   HELIX        37     40       {ECO:0000244|PDB:4F6E}.
FT   TURN         41     43       {ECO:0000244|PDB:4F6E}.
FT   HELIX        46     54       {ECO:0000244|PDB:4F6E}.
FT   HELIX        57     79       {ECO:0000244|PDB:4F6E}.
FT   HELIX        84     88       {ECO:0000244|PDB:4F6E}.
FT   HELIX        91     97       {ECO:0000244|PDB:4F6E}.
FT   HELIX       100    112       {ECO:0000244|PDB:4F6E}.
FT   HELIX       117    119       {ECO:0000244|PDB:4F6E}.
FT   TURN        120    122       {ECO:0000244|PDB:4F6E}.
FT   HELIX       127    130       {ECO:0000244|PDB:4F6E}.
FT   HELIX       133    137       {ECO:0000244|PDB:4F6E}.
FT   HELIX       140    144       {ECO:0000244|PDB:4F6E}.
FT   TURN        147    149       {ECO:0000244|PDB:4F6E}.
FT   STRAND      156    165       {ECO:0000244|PDB:4F6E}.
FT   HELIX       166    168       {ECO:0000244|PDB:4F6E}.
FT   STRAND      173    178       {ECO:0000244|PDB:4F6E}.
FT   STRAND      187    194       {ECO:0000244|PDB:4F6E}.
FT   HELIX       197    199       {ECO:0000244|PDB:4F6E}.
FT   HELIX       201    204       {ECO:0000244|PDB:4F6E}.
FT   HELIX       209    212       {ECO:0000244|PDB:4F6E}.
FT   HELIX       215    218       {ECO:0000244|PDB:4F6E}.
FT   HELIX       224    230       {ECO:0000244|PDB:4F6E}.
SQ   SEQUENCE   233 AA;  25774 MW;  88A9391FBB31D06E CRC64;
     MFAKTAAANL TKKGGLSLLS TTARRTKVTL PDLKWDFGAL EPYISGQINE LHYTKHHQTY
     VNGFNTAVDQ FQELSDLLAK EPSPANARKM IAIQQNIKFH GGGFTNHCLF WENLAPESQG
     GGEPPTGALA KAIDEQFGSL DELIKLTNTK LAGVQGSGWA FIVKNLSNGG KLDVVQTYNQ
     DTVTGPLVPL VAIDAWEHAY YLQYQNKKAD YFKAIWNVVN WKEASRRFDA GKI
//
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