P00447 (SODM_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Mn], mitochondrial
EC=1.15.1.1

Gene names

Name:	SOD2
Ordered Locus Names:	YHR008C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 manganese ion per subunit By similarity.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 10900 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the iron/manganese superoxide dismutase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Manganese Metal-binding
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	age-dependent response to reactive oxygen species involved in chronological cell aging Inferred from mutant phenotype. Source: SGD replicative cell aging Inferred from mutant phenotype. Source: SGD superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from direct assay. Source: SGD
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 26

26

Mitochondrion Ref.6

Chain

27 – 233

207

Superoxide dismutase [Mn], mitochondrial

PRO_0000032888

Sites

Metal binding

52

1

Manganese By similarity

Metal binding

107

1

Manganese By similarity

Metal binding

194

1

Manganese By similarity

Metal binding

198

1

Manganese By similarity

Amino acid modifications

Modified residue

147

1

Phosphothreonine Ref.8

Modified residue

149

1

Phosphothreonine Ref.8

Secondary structure

1

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233

Helix Strand Turn

Details...

Turn

41 – 43

3

Helix

48 – 54

7

Helix

56 – 61

6

Helix

65 – 80

16

Helix

84 – 99

16

Helix

105 – 112

8

Helix

129 – 136

8

Helix

140 – 151

12

Beta strand

160 – 165

6

Beta strand

172 – 176

5

Beta strand

187 – 193

7

Helix

197 – 199

3

Helix

201 – 204

4

Helix

208 – 214

7

Helix

215 – 218

4

Helix

221 – 229

9

Sequences

	Sequence		Length	Mass (Da)
	P00447 [UniParc]. Last modified October 23, 1986. Version 1. Checksum: 88A9391FBB31D06E	FASTA	233	25,774
	10 20 30 40 50 60 MFAKTAAANL TKKGGLSLLS TTARRTKVTL PDLKWDFGAL EPYISGQINE LHYTKHHQTY 70 80 90 100 110 120 VNGFNTAVDQ FQELSDLLAK EPSPANARKM IAIQQNIKFH GGGFTNHCLF WENLAPESQG 130 140 150 160 170 180 GGEPPTGALA KAIDEQFGSL DELIKLTNTK LAGVQGSGWA FIVKNLSNGG KLDVVQTYNQ 190 200 210 220 230 DTVTGPLVPL VAIDAWEHAY YLQYQNKKAD YFKAIWNVVN WKEASRRFDA GKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3882422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] 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: 3072251] [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]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] 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: 17761666] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND THR-149, MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

DSBYN. A00521.

RefSeq

NP_011872.1. NM_001179138.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BFR	X-ray	2.05	A	27-233	[»]
3LSU	X-ray	1.90	A/B/C/D	27-233	[»]
3RN4	X-ray	1.79	A	19-233	[»]

ProteinModelPortal

P00447.

SMR

P00447. Positions 27-231.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4905N.

IntAct

P00447. 9 interactions.

MINT

MINT-526642.

STRING

P00447.

Protein family/group databases

Allergome

867. Sac c MnSOD.

2D gel databases

UCD-2DPAGE

P00447.

Proteomic databases

PeptideAtlas

P00447.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YHR008C; YHR008C; YHR008C.

GeneID

856399.

KEGG

sce:YHR008C.

NMPDR

fig|4932.3.peg.3017.

Organism-specific databases

CYGD

YHR008c.

SGD

S000001050. SOD2.

Phylogenomic databases

eggNOG

fuNOG08676.

GeneTree

EFGT00050000003541.

HOGENOM

HBG507761.

OMA

WENLAPE.

OrthoDB

EOG42Z80G.

Gene expression databases

ArrayExpress

P00447.

Genevestigator

P00447.

GermOnline

YHR008C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]

KO

K04564.

PANTHER

PTHR11404. SODismutase. 1 hit.

Pfam

PF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000349. SODismutase. 1 hit.

PRINTS

PR01703. MNSODISMTASE.

SUPFAM

SSF46609. SODismutase. 1 hit.
SSF54719. SODismutase. 1 hit.

PROSITE

PS00088. SOD_MN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

981928.

Entry information

Entry name

SODM_YEAST

Accession

Primary (citable) accession number: P00447
Secondary accession number(s): D3DKV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 23, 1986
Last modified:	January 25, 2012
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program