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P00817

- IPYR_YEAST

UniProt

P00817 - IPYR_YEAST

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Protein

Inorganic pyrophosphatase

Gene

IPP1

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

Functioni

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791Diphosphate
Active sitei90 – 901Proton donor1 Publication
Metal bindingi116 – 1161Magnesium 1
Metal bindingi121 – 1211Magnesium 1
Metal bindingi121 – 1211Magnesium 2
Metal bindingi153 – 1531Magnesium 1

GO - Molecular functioni

  1. inorganic diphosphatase activity Source: SGD
  2. magnesium ion binding Source: InterPro

GO - Biological processi

  1. phosphate-containing compound metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YBR011C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Inorganic pyrophosphatase (EC:3.6.1.1)
Alternative name(s):
Pyrophosphate phospho-hydrolase
Short name:
PPase
Gene namesi
Name:IPP1
Synonyms:PPA, PPA1
Ordered Locus Names:YBR011C
ORF Names:YBR0202
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

SGDiS000000215. IPP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 287286Inorganic pyrophosphatasePRO_0000137588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphothreonine1 Publication
Modified residuei251 – 2511Phosphothreonine2 Publications
Modified residuei266 – 2661Phosphoserine2 Publications
Modified residuei286 – 2861Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00817.
PaxDbiP00817.
PeptideAtlasiP00817.

2D gel databases

COMPLUYEAST-2DPAGEP00817.
SWISS-2DPAGEP00817.

Expressioni

Gene expression databases

GenevestigatoriP00817.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-9338,EBI-16219

Protein-protein interaction databases

BioGridi32712. 77 interactions.
DIPiDIP-5753N.
IntActiP00817. 34 interactions.
MINTiMINT-614477.
STRINGi4932.YBR011C.

Structurei

Secondary structure

1
287
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108
Beta strandi13 – 153
Beta strandi17 – 226
Beta strandi25 – 273
Turni29 – 324
Beta strandi35 – 384
Turni39 – 424
Beta strandi43 – 508
Beta strandi58 – 603
Beta strandi62 – 643
Beta strandi69 – 713
Beta strandi75 – 773
Beta strandi85 – 873
Beta strandi91 – 966
Beta strandi106 – 1083
Turni109 – 1124
Beta strandi113 – 1153
Beta strandi117 – 1193
Beta strandi121 – 1244
Beta strandi126 – 1283
Beta strandi135 – 14410
Beta strandi146 – 1483
Beta strandi155 – 1606
Beta strandi163 – 1653
Helixi166 – 1683
Helixi172 – 1787
Helixi182 – 19211
Helixi195 – 1973
Helixi205 – 2084
Beta strandi210 – 2123
Helixi213 – 23119
Beta strandi245 – 2473
Helixi256 – 2583
Turni259 – 2613
Beta strandi266 – 2683
Helixi275 – 2784

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
117EX-ray2.15A/B2-287[»]
1E6AX-ray1.90A/B2-287[»]
1E9GX-ray1.15A/B2-287[»]
1HUJX-ray2.10A/B2-282[»]
1HUKX-ray2.20A/B2-282[»]
1M38X-ray1.80A/B1-287[»]
1PYPX-ray3.00A/B2-287[»]
1WGIX-ray2.20A/B2-287[»]
1WGJX-ray2.00A/B2-287[»]
1YPPX-ray2.40A/B2-287[»]
2IHPX-ray1.50A/B2-287[»]
2IK0X-ray1.70A/B2-287[»]
2IK1X-ray1.70A/B2-287[»]
2IK2X-ray1.80A/B2-287[»]
2IK4X-ray1.80A/B2-287[»]
2IK6X-ray1.80A/B2-287[»]
2IK7X-ray1.90A/B2-287[»]
2IK9X-ray1.50A/B2-287[»]
8PRKX-ray1.85A/B1-287[»]
ProteinModelPortaliP00817.
SMRiP00817. Positions 2-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00817.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPase family.Curated

Phylogenomic databases

eggNOGiCOG0221.
GeneTreeiENSGT00390000017004.
HOGENOMiHOG000195569.
InParanoidiP00817.
KOiK01507.
OMAiANTLEHR.
OrthoDBiEOG7K0ZP6.

Family and domain databases

Gene3Di3.90.80.10. 1 hit.
InterProiIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERiPTHR10286. PTHR10286. 1 hit.
PfamiPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF50324. SSF50324. 1 hit.
PROSITEiPS00387. PPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00817-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTYTTRQIGA KNTLEYKVYI EKDGKPVSAF HDIPLYADKE NNIFNMVVEI
60 70 80 90 100
PRWTNAKLEI TKEETLNPII QDTKKGKLRF VRNCFPHHGY IHNYGAFPQT
110 120 130 140 150
WEDPNVSHPE TKAVGDNDPI DVLEIGETIA YTGQVKQVKA LGIMALLDEG
160 170 180 190 200
ETDWKVIAID INDPLAPKLN DIEDVEKYFP GLLRATNEWF RIYKIPDGKP
210 220 230 240 250
ENQFAFSGEA KNKKYALDII KETHDSWKQL IAGKSSDSKG IDLTNVTLPD
260 270 280
TPTYSKAASD AIPPASPKAD APIDKSIDKW FFISGSV
Length:287
Mass (Da):32,300
Last modified:July 24, 2007 - v4
Checksum:i1DC19A702A389BA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411N → D AA sequence (PubMed:340461)Curated
Sequence conflicti72 – 721D → N AA sequence (PubMed:340461)Curated
Sequence conflicti75 – 751Missing AA sequence (PubMed:340461)Curated
Sequence conflicti124 – 1241E → Q AA sequence (PubMed:340461)Curated
Sequence conflicti137 – 1371Q → E AA sequence (PubMed:340461)Curated
Sequence conflicti187 – 1871N → D AA sequence (PubMed:340461)Curated
Sequence conflicti225 – 2251D → N AA sequence (PubMed:340461)Curated
Sequence conflicti267 – 2671P → L in CAA31629. (PubMed:2849749)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13253 Genomic DNA. Translation: CAA31629.1.
Z35880 Genomic DNA. Translation: CAA84949.1.
AY692953 Genomic DNA. Translation: AAT92972.1.
BK006936 Genomic DNA. Translation: DAA07132.1.
PIRiS45864. PWBY.
RefSeqiNP_009565.1. NM_001178359.1.

Genome annotation databases

EnsemblFungiiYBR011C; YBR011C; YBR011C.
GeneIDi852296.
KEGGisce:YBR011C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13253 Genomic DNA. Translation: CAA31629.1 .
Z35880 Genomic DNA. Translation: CAA84949.1 .
AY692953 Genomic DNA. Translation: AAT92972.1 .
BK006936 Genomic DNA. Translation: DAA07132.1 .
PIRi S45864. PWBY.
RefSeqi NP_009565.1. NM_001178359.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
117E X-ray 2.15 A/B 2-287 [» ]
1E6A X-ray 1.90 A/B 2-287 [» ]
1E9G X-ray 1.15 A/B 2-287 [» ]
1HUJ X-ray 2.10 A/B 2-282 [» ]
1HUK X-ray 2.20 A/B 2-282 [» ]
1M38 X-ray 1.80 A/B 1-287 [» ]
1PYP X-ray 3.00 A/B 2-287 [» ]
1WGI X-ray 2.20 A/B 2-287 [» ]
1WGJ X-ray 2.00 A/B 2-287 [» ]
1YPP X-ray 2.40 A/B 2-287 [» ]
2IHP X-ray 1.50 A/B 2-287 [» ]
2IK0 X-ray 1.70 A/B 2-287 [» ]
2IK1 X-ray 1.70 A/B 2-287 [» ]
2IK2 X-ray 1.80 A/B 2-287 [» ]
2IK4 X-ray 1.80 A/B 2-287 [» ]
2IK6 X-ray 1.80 A/B 2-287 [» ]
2IK7 X-ray 1.90 A/B 2-287 [» ]
2IK9 X-ray 1.50 A/B 2-287 [» ]
8PRK X-ray 1.85 A/B 1-287 [» ]
ProteinModelPortali P00817.
SMRi P00817. Positions 2-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32712. 77 interactions.
DIPi DIP-5753N.
IntActi P00817. 34 interactions.
MINTi MINT-614477.
STRINGi 4932.YBR011C.

2D gel databases

COMPLUYEAST-2DPAGE P00817.
SWISS-2DPAGE P00817.

Proteomic databases

MaxQBi P00817.
PaxDbi P00817.
PeptideAtlasi P00817.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR011C ; YBR011C ; YBR011C .
GeneIDi 852296.
KEGGi sce:YBR011C.

Organism-specific databases

SGDi S000000215. IPP1.

Phylogenomic databases

eggNOGi COG0221.
GeneTreei ENSGT00390000017004.
HOGENOMi HOG000195569.
InParanoidi P00817.
KOi K01507.
OMAi ANTLEHR.
OrthoDBi EOG7K0ZP6.

Enzyme and pathway databases

BioCyci YEAST:YBR011C-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00817.
NextBioi 970952.
PROi P00817.

Gene expression databases

Genevestigatori P00817.

Family and domain databases

Gene3Di 3.90.80.10. 1 hit.
InterProi IPR008162. Pyrophosphatase.
[Graphical view ]
PANTHERi PTHR10286. PTHR10286. 1 hit.
Pfami PF00719. Pyrophosphatase. 1 hit.
[Graphical view ]
SUPFAMi SSF50324. SSF50324. 1 hit.
PROSITEi PS00387. PPASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    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. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-287.
  6. Cited for: PROTEIN SEQUENCE OF 26-36 AND 240-252.
    Strain: ATCC 204508 / S288c.
  7. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 240-250.
    Strain: ATCC 38531 / Y41.
  8. "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] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE TYR-90.
  9. "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] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251 AND SER-286, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65 AND SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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).
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  18. 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).
  19. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF MUTANTS LYS-79 AND LYS-118.
  20. "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] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO E.COLI AND K.LACTIS PPASES.

Entry informationi

Entry nameiIPYR_YEAST
AccessioniPrimary (citable) accession number: P00817
Secondary accession number(s): D6VQ12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 24, 2007
Last modified: October 29, 2014
This is version 163 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 68400 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3