Reviewed, UniProtKB/Swiss-Prot P00817 (IPYR_YEAST)

Names and origin

Protein names

Recommended name:
    Inorganic pyrophosphatase
    EC=3.6.1.1
Alternative name(s):
    Pyrophosphate phospho-hydrolase
      Short name=PPase

Gene names

Name:	IPP1
Synonyms:	PPA, PPA1
Ordered Locus Names:	YBR011C
ORF Names:	YBR0202

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	287 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)

Catalytic activity	Diphosphate + H(2)O = 2 phosphate.
Cofactor	Binds 4 magnesium ions per subunit. Other metal ions can support activity, but at a lower rate. Two magnesium ions are required for the activation of the enzyme and are present before substrate binds, two additional magnesium ions form complexes with substrate and product By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 68400 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the PPase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	phosphate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Traceable author statement. Source: SGD
Molecular function	inorganic diphosphatase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AUS1	Q08409	1	EBI-9338,EBI-35723
ESS1	P22696	1	EBI-9338,EBI-6679
RSP5	P39940	1	EBI-9338,EBI-16219
SSM4	P40318	1	EBI-9338,EBI-18208
URN1	Q06525	1	EBI-9338,EBI-35138

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 287

286

Inorganic pyrophosphatase

PRO_0000137588

Sites

Active site

90

1

Proton donor

Metal binding

116

1

Magnesium 1

Metal binding

121

1

Magnesium 1

Metal binding

121

1

Magnesium 2

Metal binding

153

1

Magnesium 1

Binding site

79

1

Inorganic pyrophosphate

Amino acid modifications

Modified residue

61

1

Phosphothreonine

Modified residue

65

1

Phosphothreonine

Modified residue

247

1

Phosphothreonine

Modified residue

251

1

Phosphothreonine

Modified residue

253

1

Phosphothreonine

Modified residue

255

1

Phosphoserine

Modified residue

266

1

Phosphoserine

Modified residue

286

1

Phosphoserine

Experimental info

Sequence conflict

41

1

N → D AA sequence Ref.4

Sequence conflict

72

1

D → N AA sequence Ref.4

Sequence conflict

75

1

Missing AA sequence Ref.4

Sequence conflict

124

1

E → Q AA sequence Ref.4

Sequence conflict

137

1

Q → E AA sequence Ref.4

Sequence conflict

187

1

N → D AA sequence Ref.4

Sequence conflict

225

1

D → N AA sequence Ref.4

Sequence conflict

267

1

P → L in CAA31629. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

287

Helix Strand Turn

Details...

Beta strand

3 – 13

11

Beta strand

17 – 22

6

Beta strand

25 – 27

3

Turn

29 – 32

4

Beta strand

35 – 38

4

Helix

39 – 41

3

Beta strand

43 – 50

8

Beta strand

58 – 60

3

Beta strand

62 – 64

3

Beta strand

69 – 71

3

Beta strand

91 – 96

6

Beta strand

106 – 108

3

Turn

109 – 112

4

Beta strand

113 – 115

3

Beta strand

121 – 124

4

Beta strand

135 – 144

10

Beta strand

146 – 148

3

Beta strand

155 – 160

6

Helix

166 – 168

3

Helix

172 – 178

7

Helix

182 – 192

11

Helix

195 – 197

3

Beta strand

203 – 205

3

Helix

206 – 208

3

Beta strand

210 – 212

3

Helix

213 – 231

19

Beta strand

245 – 247

3

Helix

256 – 258

3

Turn

259 – 261

3

Beta strand

266 – 268

3

Helix

275 – 278

4

Sequences

	Sequence		Length	Mass (Da)
	P00817-1 [UniParc]. Last modified July 24, 2007. Version 4. Checksum: 1DC19A702A389BA9	FASTA	287	32,300
	10 20 30 40 50 60 MTYTTRQIGA KNTLEYKVYI EKDGKPVSAF HDIPLYADKE NNIFNMVVEI PRWTNAKLEI 70 80 90 100 110 120 TKEETLNPII QDTKKGKLRF VRNCFPHHGY IHNYGAFPQT WEDPNVSHPE TKAVGDNDPI 130 140 150 160 170 180 DVLEIGETIA YTGQVKQVKA LGIMALLDEG ETDWKVIAID INDPLAPKLN DIEDVEKYFP 190 200 210 220 230 240 GLLRATNEWF RIYKIPDGKP ENQFAFSGEA KNKKYALDII KETHDSWKQL IAGKSSDSKG 250 260 270 280 IDLTNVTLPD TPTYSKAASD AIPPASPKAD APIDKSIDKW FFISGSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, molecular characterization and chromosome localization of the inorganic pyrophosphatase (PPA) gene from S. cerevisiae." Kolakowski L.F. Jr., Schloesser M., Cooperman B.S. Nucleic Acids Res. 16:10441-10452(1988) [PubMed: 2849749] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26109 / X2180.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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.
[4]	"Covalent structural analysis of yeast inorganic pyrophosphatase." Cohen S.A., Sterner R., Keim P.S., Heinrikson R.L. J. Biol. Chem. 253:889-897(1978) [PubMed: 340461] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-287.
[5]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-36 AND 240-252. Strain: ATCC 204508 / S288c.
[6]	"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae." Norbeck J., Blomberg A. FEMS Microbiol. Lett. 137:1-8(1996) [PubMed: 8935650] [Abstract] Cited for: PROTEIN SEQUENCE OF 240-250. Strain: ATCC 38531 / Y41.
[7]	"Tyrosine-89 is important for enzymatic activity of S. cerevisiae inorganic pyrophosphatase." Raznikov A.V., Sklyankina V.A., Avaeva S.M. FEBS Lett. 308:62-64(1992) [PubMed: 1322842] [Abstract] Cited for: ACTIVE SITE TYR-90.
[8]	"Identification of an arginine important for enzymatic activity within the covalent structure of yeast inorganic pyrophosphatase." Bond M.W., Chiu N.Y., Cooperman B.S. Biochemistry 19:94-102(1980) [PubMed: 6101539] [Abstract] Cited for: ACTIVE SITE.
[9]	"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].
[10]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251 AND SER-286, MASS SPECTROMETRY.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61 AND SER-266, MASS SPECTROMETRY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65; THR-247; THR-251; THR-253; SER-255 AND SER-266, MASS SPECTROMETRY.
[14]	"X-ray diffraction study of inorganic pyrophosphatase from baker's yeast at the 3-A resolution." Arutiunian E.G., Terzian S.S., Voronova A.A., Kuranova I.P., Smirnova E.A., Vainstein B.K., Hohne W.E., Hansen G. Dokl. Akad. Nauk SSSR 258:1481-1492(1981) Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[15]	"The structural basis for pyrophosphatase catalysis." Heikinheimo P., Lehtonen J., Baykov A., Lahti R., Cooperman B.S., Goldman A. Structure 4:1491-1508(1996) [PubMed: 8994974] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[16]	Swaminathan K., Cooperman B.S., Lahti R., Voet D. Submitted (DEC-1997) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[17]	"The R78K and D117E active-site variants of Saccharomyces cerevisiae soluble inorganic pyrophosphatase: structural studies and mechanistic implications." Tuominen V., Heikinheimo P., Kajander T., Torkkel T., Hyytia T., Kapyla J., Lahti R., Cooperman B.S., Goldman A. J. Mol. Biol. 284:1565-1580(1998) [PubMed: 9878371] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF MUTANTS LYS-79 AND LYS-118.
[18]	"Conservation of functional residues between yeast and E. coli inorganic pyrophosphatases." Lahti R., Kolakowski L.F. Jr., Heinonen J., Vihinen M., Pohjanoksa K., Cooperman B.S. Biochim. Biophys. Acta 1038:338-345(1990) [PubMed: 2160278] [Abstract] Cited for: SIMILARITY TO E.COLI AND K.LACTIS PPASES.
+	Additional comput