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UniProtKB/Swiss-Prot entry P00817


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IPYR_YEAST
Primary accession number P00817
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 24, 2007 (Sequence version 4)
Annotations were last modified on    July 22, 2008 (Entry version 105)
Name and origin of the protein
Protein name Inorganic pyrophosphatase
Synonyms EC 3.6.1.1
Pyrophosphate phospho-hydrolase
PPase
Gene name
Name: IPP1
Synonyms: PPA, PPA1
OrderedLocusNames: YBR011C
ORFNames: YBR0202
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 26109 / X2180;
DOI=10.1093/nar/16.22.10441; PubMed=2849749 [NCBI, ExPASy, EBI, Israel, Japan]
Kolakowski L.F. Jr., Schloesser M., Cooperman B.S.;
"Cloning, molecular characterization and chromosome localization of the inorganic pyrophosphatase (PPA) gene from S. cerevisiae.";
Nucleic Acids Res. 16:10441-10452(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
PROTEIN SEQUENCE OF 2-287.
PubMed=340461 [NCBI, ExPASy, EBI, Israel, Japan]
Cohen S.A., Sterner R., Keim P.S., Heinrikson R.L.;
"Covalent structural analysis of yeast inorganic pyrophosphatase.";
J. Biol. Chem. 253:889-897(1978).
[5]
PROTEIN SEQUENCE OF 26-36 AND 240-252.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[6]
PROTEIN SEQUENCE OF 240-250.
STRAIN=ATCC 38531 / Y41;
DOI=10.1016/0378-1097(96)00006-7; PubMed=8935650 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 137:1-8(1996).
[7]
ACTIVE SITE TYR-90.
DOI=10.1016/0014-5793(92)81051-M; PubMed=1322842 [NCBI, ExPASy, EBI, Israel, Japan]
Raznikov A.V., Sklyankina V.A., Avaeva S.M.;
"Tyrosine-89 is important for enzymatic activity of S. cerevisiae inorganic pyrophosphatase.";
FEBS Lett. 308:62-64(1992).
[8]
ACTIVE SITE.
DOI=10.1021/bi00542a015; PubMed=6101539 [NCBI, ExPASy, EBI, Israel, Japan]
Bond M.W., Chiu N.Y., Cooperman B.S.;
"Identification of an arginine important for enzymatic activity within the covalent structure of yeast inorganic pyrophosphatase.";
Biochemistry 19:94-102(1980).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251 AND SER-286, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61 AND SER-266, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65; THR-247; THR-251; THR-253; SER-255 AND SER-266, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 0:0-0(2008).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Arutiunian E.G., Terzian S.S., Voronova A.A., Kuranova I.P., Smirnova E.A., Vainstein B.K., Hohne W.E., Hansen G.;
"X-ray diffraction study of inorganic pyrophosphatase from baker's yeast at the 3-A resolution.";
Dokl. Akad. Nauk SSSR 258:1481-1492(1981).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1016/S0969-2126(96)00155-4; PubMed=8994974 [NCBI, ExPASy, EBI, Israel, Japan]
Heikinheimo P., Lehtonen J., Baykov A., Lahti R., Cooperman B.S., Goldman A.;
"The structural basis for pyrophosphatase catalysis.";
Structure 4:1491-1508(1996).
[16]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Swaminathan K., Cooperman B.S., Lahti R., Voet D.;
Submitted (DEC-1997) to the PDB data bank.
[17]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF MUTANTS LYS-79 AND LYS-118.
DOI=10.1006/jmbi.1998.2266; PubMed=9878371 [NCBI, ExPASy, EBI, Israel, Japan]
Tuominen V., Heikinheimo P., Kajander T., Torkkel T., Hyytia T., Kapyla J., Lahti R., Cooperman B.S., Goldman A.;
"The R78K and D117E active-site variants of Saccharomyces cerevisiae soluble inorganic pyrophosphatase: structural studies and mechanistic implications.";
J. Mol. Biol. 284:1565-1580(1998).
[18]
SIMILARITY TO E.COLI AND K.LACTIS PPASES.
DOI=10.1016/0167-4838(90)90246-C; PubMed=2160278 [NCBI, ExPASy, EBI, Israel, Japan]
Lahti R., Kolakowski L.F. Jr., Heinonen J., Vihinen M., Pohjanoksa K., Cooperman B.S.;
"Conservation of functional residues between yeast and E. coli inorganic pyrophosphatases.";
Biochim. Biophys. Acta 1038:338-345(1990).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X13253; CAA31629.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35880; CAA84949.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692953; AAT92972.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S45864; PWBY.
RefSeq NP_009565.1; -.
3D structure databases
PDB
117E; X-ray; 2.15 A; A/B=1-287.[ExPASy / RCSB / EBI]
1E6A; X-ray; 1.90 A; A/B=1-287.[ExPASy / RCSB / EBI]
1E9G; X-ray; 1.15 A; A/B=1-287.[ExPASy / RCSB / EBI]
1HUJ; X-ray; 2.10 A; A/B=1-282.[ExPASy / RCSB / EBI]
1HUK; X-ray; 2.20 A; A/B=1-282.[ExPASy / RCSB / EBI]
1M38; X-ray; 1.80 A; A/B=1-287.[ExPASy / RCSB / EBI]
1PYP; X-ray; 3.00 A; A/B=2-287.[ExPASy / RCSB / EBI]
1WGI; X-ray; 2.20 A; A/B=1-287.[ExPASy / RCSB / EBI]
1WGJ; X-ray; 2.00 A; A/B=1-287.[ExPASy / RCSB / EBI]
1YPP; X-ray; 2.40 A; A/B=1-287.[ExPASy / RCSB / EBI]
2IHP; X-ray; 1.50 A; A/B=2-287.[ExPASy / RCSB / EBI]
2IK0; X-ray; 1.70 A; A/B=2-287.[ExPASy / RCSB / EBI]
2IK1; X-ray; 1.70 A; A/B=2-287.[ExPASy / RCSB / EBI]
2IK2; X-ray; 1.80 A; A/B=2-287.[ExPASy / RCSB / EBI]
2IK4; X-ray; 1.80 A; A/B=2-287.[ExPASy / RCSB / EBI]
2IK6; X-ray; 1.80 A; A/B=2-287.[ExPASy / RCSB / EBI]
2IK7; X-ray; 1.90 A; A/B=2-287.[ExPASy / RCSB / EBI]
2IK9; X-ray; 1.50 A; A/B=2-287.[ExPASy / RCSB / EBI]
8PRK; X-ray; 1.85 A; A/B=1-287.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 117E; -.
1E6A; -.
1E9G; -.
1HUJ; -.
1HUK; -.
1M38; -.
1PYP; -.
1WGI; -.
1WGJ; -.
1YPP; -.
2IHP; -.
2IK0; -.
2IK1; -.
2IK2; -.
2IK4; -.
2IK6; -.
2IK7; -.
2IK9; -.
8PRK; -.
ModBase P00817.
Protein-protein interaction databases
DIP DIP:5753N; -.
IntAct P00817; -.
2D gel databases
SWISS-2DPAGE P00817; -.
COMPLUYEAST-2DPAGE P00817; -.
Organism-specific databases
CYGD YBR011c; -.
SGD S000000215; IPP1.
Yeast-GFP YBR011C.
Gene expression databases
ArrayExpress P00817; -.
GermOnline YBR011C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from SGD).
GO:0004427; Molecular function: inorganic diphosphatase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006796; Biological process: phosphate metabolic process (inferred by curator from SGD).
QuickGo view.
Family and domain databases
InterPro IPR008162; Pyrophosphatase.
Graphical view of domain structure.
PANTHER PTHR10286; Pyrophosphatase; 1.
Pfam PF00719; Pyrophosphatase; 1.
Pfam graphical view of domain structure.
ProDom PD002014; Inorg_pphsph; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00387; PPASE; 1.
BLOCKS P00817.
Proteomic databases
PeptideAtlas P00817; -.
Genome annotation databases
Ensembl YBR011C; Saccharomyces cerevisiae. [Contig view]
GeneID 852296; -.
GenomeReviews Y13134_GR; YBR011C.
KEGG sce:YBR011C; -.
NMPDR fig|4932.3.peg.260; -.
Phylogenomic databases
HOGENOM P00817; -.
Other
LinkHub P00817; -.
ProtoNet P00817.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   287  286     Inorganic pyrophosphatase. PRO_0000137588
ACT_SITE   90    90        Proton donor. 
METAL   116   116        Magnesium 1. 
METAL   121   121        Magnesium 1. 
METAL   121   121        Magnesium 2. 
METAL   153   153        Magnesium 1. 
BINDING   79    79        Inorganic pyrophosphate. 
MOD_RES   61    61        Phosphothreonine. 
MOD_RES   65    65        Phosphothreonine. 
MOD_RES   247   247        Phosphothreonine. 
MOD_RES   251   251        Phosphothreonine. 
MOD_RES   253   253        Phosphothreonine. 
MOD_RES   255   255        Phosphoserine. 
MOD_RES   266   266        Phosphoserine. 
MOD_RES   286   286        Phosphoserine. 
CONFLICT   41    41        N -> D (in Ref. 4; AA sequence). 
CONFLICT   72    72        D -> N (in Ref. 4; AA sequence). 
CONFLICT   75    75        Missing (in Ref. 4; AA sequence). 
CONFLICT   124   124        E -> Q (in Ref. 4; AA sequence). 
CONFLICT   137   137        Q -> E (in Ref. 4; AA sequence). 
CONFLICT   187   187        N -> D (in Ref. 4; AA sequence). 
CONFLICT   225   225        D -> N (in Ref. 4; AA sequence). 
CONFLICT   267   267        P -> L (in Ref. 1; CAA31629). 
STRAND   3    13  11      
STRAND   17    22  6      
STRAND   25    27  3      
TURN   29    32  4      
STRAND   35    38  4      
HELIX   39    41  3      
STRAND   43    50  8      
STRAND   58    60  3      
STRAND   62    64  3      
STRAND   69    71  3      
STRAND   91    96  6      
STRAND   106   108  3      
TURN   109   112  4      
STRAND   113   115  3      
STRAND   121   124  4      
STRAND   135   144  10      
STRAND   146   148  3      
STRAND   155   160  6      
HELIX   166   168  3      
HELIX   172   178  7      
HELIX   182   192  11      
HELIX   195   197  3      
STRAND   203   205  3      
HELIX   206   208  3      
STRAND   210   212  3      
HELIX   213   231  19      
STRAND   245   247  3      
HELIX   256   258  3      
TURN   259   261  3      
STRAND   266   268  3      
HELIX   275   278  4      
Sequence information
Length: 287 AA [This is the length of the unprocessed precursor] Molecular weight: 32300 Da [This is the MW of the unprocessed precursor] CRC64: 1DC19A702A389BA9 [This is a checksum on the sequence]
        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 

P00817 in FASTA format

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