SODM_YEAST
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 03-AUG-2022, entry version 205.
DE RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:P0A0J3};
DE Flags: Precursor;
GN Name=SOD2; OrderedLocusNames=YHR008C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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., Grivell L.A.,
RA Slater E.C.;
RT "Nucleotide sequence analysis of the nuclear gene coding for manganese
RT superoxide dismutase of yeast mitochondria, a gene previously assumed to
RT 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., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT 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 from
RT 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., Dephoure N.,
RA 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 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 -!- 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 family.
CC {ECO:0000305}.
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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 AlphaFoldDB; P00447; -.
DR SMR; P00447; -.
DR BioGRID; 36435; 235.
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; YHR008C.
DR GeneID; 856399; -.
DR KEGG; sce:YHR008C; -.
DR SGD; S000001050; SOD2.
DR VEuPathDB; FungiDB:YHR008C; -.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_2_1_1; -.
DR InParanoid; P00447; -.
DR OMA; KWGSFDK; -.
DR BioCyc; YEAST:MON3O-1642; -.
DR Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
DR EvolutionaryTrace; P00447; -.
DR PRO; PR:P00447; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P00447; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:SGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Direct protein sequencing; Manganese;
KW Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 27..233
FT /note="Superoxide dismutase [Mn], mitochondrial"
FT /id="PRO_0000032888"
FT BINDING 52
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 107
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P04179"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:4F6E"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 57..79
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4F6E"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:4F6E"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4F6E"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4F6E"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:4F6E"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:4F6E"
FT HELIX 224..230
FT /evidence="ECO:0007829|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
