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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

SOD2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521ManganeseBy similarity
Metal bindingi107 – 1071ManganeseBy similarity
Metal bindingi194 – 1941ManganeseBy similarity
Metal bindingi198 – 1981ManganeseBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • superoxide dismutase activity Source: SGD

GO - Biological processi

  • age-dependent response to oxidative stress involved in chronological cell aging Source: SGD
  • age-dependent response to reactive oxygen species involved in chronological cell aging Source: SGD
  • reactive oxygen species metabolic process Source: SGD
  • replicative cell aging Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-1642.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Gene namesi
Name:SOD2
Ordered Locus Names:YHR008C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR008C.
SGDiS000001050. SOD2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Protein family/group databases

Allergomei867. Sac c MnSOD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626Mitochondrion1 PublicationAdd
BLAST
Chaini27 – 233207Superoxide dismutase [Mn], mitochondrialPRO_0000032888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei147 – 1471PhosphothreonineCombined sources
Modified residuei149 – 1491PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00447.
PRIDEiP00447.
TopDownProteomicsiP00447.

2D gel databases

UCD-2DPAGEP00447.

PTM databases

iPTMnetiP00447.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi36435. 85 interactions.
DIPiDIP-4905N.
IntActiP00447. 7 interactions.
MINTiMINT-526642.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 404Combined sources
Turni41 – 433Combined sources
Helixi46 – 549Combined sources
Helixi56 – 8025Combined sources
Helixi84 – 11229Combined sources
Helixi117 – 1193Combined sources
Turni120 – 1223Combined sources
Helixi127 – 13711Combined sources
Helixi140 – 15213Combined sources
Beta strandi156 – 16510Combined sources
Helixi166 – 1683Combined sources
Beta strandi172 – 1787Combined sources
Beta strandi187 – 1948Combined sources
Helixi197 – 1993Combined sources
Helixi201 – 2044Combined sources
Helixi208 – 2158Combined sources
Helixi216 – 2183Combined sources
Helixi221 – 23010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BFRX-ray2.05A27-233[»]
3LSUX-ray1.90A/B/C/D27-233[»]
3RN4X-ray1.79A19-233[»]
4E4EX-ray1.88A/B/C/D27-233[»]
4F6EX-ray1.60A/B/C/D28-233[»]
ProteinModelPortaliP00447.
SMRiP00447. Positions 27-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00447.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
InParanoidiP00447.
KOiK04564.
OMAiRYDELEP.
OrthoDBiEOG7W9S5R.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAKTAAANL TKKGGLSLLS TTARRTKVTL PDLKWDFGAL EPYISGQINE
60 70 80 90 100
LHYTKHHQTY VNGFNTAVDQ FQELSDLLAK EPSPANARKM IAIQQNIKFH
110 120 130 140 150
GGGFTNHCLF WENLAPESQG GGEPPTGALA KAIDEQFGSL DELIKLTNTK
160 170 180 190 200
LAGVQGSGWA FIVKNLSNGG KLDVVQTYNQ DTVTGPLVPL VAIDAWEHAY
210 220 230
YLQYQNKKAD YFKAIWNVVN WKEASRRFDA GKI
Length:233
Mass (Da):25,774
Last modified:October 23, 1986 - v1
Checksum:i88A9391FBB31D06E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02156 Genomic DNA. Translation: CAA26092.1.
U10400 Genomic DNA. Translation: AAB68939.1.
M24079 Genomic DNA. Translation: AAA35065.1.
AY557821 Genomic DNA. Translation: AAS56147.1.
BK006934 Genomic DNA. Translation: DAA06697.1.
PIRiA00521. DSBYN.
RefSeqiNP_011872.1. NM_001179138.1.

Genome annotation databases

EnsemblFungiiYHR008C; YHR008C; YHR008C.
GeneIDi856399.
KEGGisce:YHR008C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02156 Genomic DNA. Translation: CAA26092.1.
U10400 Genomic DNA. Translation: AAB68939.1.
M24079 Genomic DNA. Translation: AAA35065.1.
AY557821 Genomic DNA. Translation: AAS56147.1.
BK006934 Genomic DNA. Translation: DAA06697.1.
PIRiA00521. DSBYN.
RefSeqiNP_011872.1. NM_001179138.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BFRX-ray2.05A27-233[»]
3LSUX-ray1.90A/B/C/D27-233[»]
3RN4X-ray1.79A19-233[»]
4E4EX-ray1.88A/B/C/D27-233[»]
4F6EX-ray1.60A/B/C/D28-233[»]
ProteinModelPortaliP00447.
SMRiP00447. Positions 27-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36435. 85 interactions.
DIPiDIP-4905N.
IntActiP00447. 7 interactions.
MINTiMINT-526642.

Protein family/group databases

Allergomei867. Sac c MnSOD.

PTM databases

iPTMnetiP00447.

2D gel databases

UCD-2DPAGEP00447.

Proteomic databases

MaxQBiP00447.
PRIDEiP00447.
TopDownProteomicsiP00447.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR008C; YHR008C; YHR008C.
GeneIDi856399.
KEGGisce:YHR008C.

Organism-specific databases

EuPathDBiFungiDB:YHR008C.
SGDiS000001050. SOD2.

Phylogenomic databases

GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
InParanoidiP00447.
KOiK04564.
OMAiRYDELEP.
OrthoDBiEOG7W9S5R.

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-1642.
ReactomeiR-SCE-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

EvolutionaryTraceiP00447.
PROiP00447.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron-sulphur protein."
    Marres C.A.M., van Loon A.P.G.M., Oudshoorn P., van Steeg H., Grivell L.A., Slater E.C.
    Eur. J. Biochem. 147:153-161(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Functional expression of the yeast Mn-superoxide dismutase gene in Escherichia coli requires deletion of the signal peptide sequence."
    Schrank I.S., Sims P.F., Oliver S.G.
    Gene 73:121-130(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
  6. "The complete amino acid sequence of manganese-superoxide dismutase from Saccharomyces cerevisae."
    Ditlow C., Johansen J.T., Martin B.M., Svendsen I.
    Carlsberg Res. Commun. 47:81-91(1982)
    Cited for: PROTEIN SEQUENCE OF 27-233.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
    Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
    Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND THR-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiSODM_YEAST
AccessioniPrimary (citable) accession number: P00447
Secondary accession number(s): D3DKV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 23, 1986
Last modified: July 6, 2016
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10900 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.