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Protein

Inorganic pyrophosphatase

Gene

ppa

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mg2+Note: Binds 4 Mg2+ ions per subunit. Other metal ions can support activity, but at a lower rate. Two Mg2+ ions are required for the activation of the enzyme and are present before substrate binds, two additional Mg2+ ions form complexes with substrate and product.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Magnesium 1
Metal bindingi71 – 711Magnesium 1
Metal bindingi71 – 711Magnesium 2
Metal bindingi103 – 1031Magnesium 1

GO - Molecular functioni

  • inorganic diphosphatase activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • triphosphatase activity Source: EcoCyc
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:INORGPYROPHOSPHAT-MONOMER.
ECOL316407:JW4185-MONOMER.
MetaCyc:INORGPYROPHOSPHAT-MONOMER.
BRENDAi3.6.1.1. 2026.

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:ppa
Ordered Locus Names:b4226, JW4185
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10755. ppa.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211E → D: 16% activity.
Mutagenesisi30 – 301K → R: 2% activity.
Mutagenesisi32 – 321E → D: 6% activity.
Mutagenesisi44 – 441R → K: 10% activity.
Mutagenesisi52 – 521Y → F: 64% activity.
Mutagenesisi56 – 561Y → F: 7% activity.
Mutagenesisi66 – 661D → E: 6% activity.
Mutagenesisi68 – 681D → E: 1% activity.
Mutagenesisi71 – 711D → E: No activity.
Mutagenesisi98 – 981D → E: 22% activity.
Mutagenesisi98 – 981D → V: No activity.
Mutagenesisi99 – 991E → V: 33% activity.
Mutagenesisi103 – 1031D → E: 3% activity.
Mutagenesisi103 – 1031D → V: No activity.
Mutagenesisi105 – 1051K → I: No activity.
Mutagenesisi105 – 1051K → R: 3% activity.
Mutagenesisi142 – 1421Y → F: 22% activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 176175Inorganic pyrophosphatasePRO_0000137495Add
BLAST

Proteomic databases

EPDiP0A7A9.
PaxDbiP0A7A9.
PRIDEiP0A7A9.

2D gel databases

SWISS-2DPAGEP0A7A9.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi4259312. 36 interactions.
DIPiDIP-36217N.
IntActiP0A7A9. 36 interactions.
MINTiMINT-1226708.
STRINGi511145.b4226.

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Beta strandi8 – 114Combined sources
Turni12 – 143Combined sources
Beta strandi15 – 228Combined sources
Beta strandi28 – 336Combined sources
Turni35 – 373Combined sources
Beta strandi40 – 456Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 586Combined sources
Beta strandi65 – 684Combined sources
Beta strandi71 – 744Combined sources
Beta strandi85 – 9814Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi105 – 1106Combined sources
Turni112 – 1143Combined sources
Turni117 – 1204Combined sources
Helixi124 – 1263Combined sources
Helixi129 – 14113Combined sources
Turni142 – 1454Combined sources
Beta strandi151 – 1577Combined sources
Helixi159 – 17517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FAJX-ray2.15A2-176[»]
1I40X-ray1.10A2-176[»]
1I6TX-ray1.20A2-176[»]
1IGPX-ray2.20A2-176[»]
1INOX-ray2.20A2-176[»]
1IPWX-ray2.30A/B2-176[»]
1JFDX-ray2.20A/B2-176[»]
1MJWX-ray1.95A/B2-176[»]
1MJXX-ray2.15A/B2-176[»]
1MJYX-ray2.10A/B2-176[»]
1MJZX-ray2.20A2-176[»]
1OBWX-ray1.90A/B/C2-176[»]
2AU6X-ray1.20A2-176[»]
2AU7X-ray1.05A2-176[»]
2AU8X-ray1.65A2-176[»]
2AU9X-ray1.30A2-176[»]
2AUUX-ray1.22A2-176[»]
2EIPX-ray2.20A/B2-176[»]
4UM4X-ray2.65A/B/C1-176[»]
ProteinModelPortaliP0A7A9.
SMRiP0A7A9. Positions 2-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7A9.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPase family.Curated

Phylogenomic databases

eggNOGiENOG4105F0N. Bacteria.
COG0221. LUCA.
HOGENOMiHOG000236473.
InParanoidiP0A7A9.
KOiK01507.
OMAiPVALMKM.
OrthoDBiEOG6NKR4X.
PhylomeDBiP0A7A9.

Family and domain databases

Gene3Di3.90.80.10. 1 hit.
HAMAPiMF_00209. Inorganic_PPase.
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.

P0A7A9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLNVPAGK DLPEDIYVVI EIPANADPIK YEIDKESGAL FVDRFMSTAM
60 70 80 90 100
FYPCNYGYIN HTLSLDGDPV DVLVPTPYPL QPGSVIRCRP VGVLKMTDEA
110 120 130 140 150
GEDAKLVAVP HSKLSKEYDH IKDVNDLPEL LKAQIAHFFE HYKDLEKGKW
160 170
VKVEGWENAE AAKAEIVASF ERAKNK
Length:176
Mass (Da):19,704
Last modified:January 23, 2007 - v2
Checksum:i4C97E51F3BE650DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23550 Unassigned DNA. Translation: AAB88583.1.
U14003 Genomic DNA. Translation: AAA97123.1.
U00096 Genomic DNA. Translation: AAC77183.1.
AP009048 Genomic DNA. Translation: BAE78227.1.
PIRiA27648. PWEC.
RefSeqiNP_418647.1. NC_000913.3.
WP_000055075.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77183; AAC77183; b4226.
BAE78227; BAE78227; BAE78227.
GeneIDi948748.
KEGGiecj:JW4185.
eco:b4226.
PATRICi32124027. VBIEscCol129921_4358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23550 Unassigned DNA. Translation: AAB88583.1.
U14003 Genomic DNA. Translation: AAA97123.1.
U00096 Genomic DNA. Translation: AAC77183.1.
AP009048 Genomic DNA. Translation: BAE78227.1.
PIRiA27648. PWEC.
RefSeqiNP_418647.1. NC_000913.3.
WP_000055075.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FAJX-ray2.15A2-176[»]
1I40X-ray1.10A2-176[»]
1I6TX-ray1.20A2-176[»]
1IGPX-ray2.20A2-176[»]
1INOX-ray2.20A2-176[»]
1IPWX-ray2.30A/B2-176[»]
1JFDX-ray2.20A/B2-176[»]
1MJWX-ray1.95A/B2-176[»]
1MJXX-ray2.15A/B2-176[»]
1MJYX-ray2.10A/B2-176[»]
1MJZX-ray2.20A2-176[»]
1OBWX-ray1.90A/B/C2-176[»]
2AU6X-ray1.20A2-176[»]
2AU7X-ray1.05A2-176[»]
2AU8X-ray1.65A2-176[»]
2AU9X-ray1.30A2-176[»]
2AUUX-ray1.22A2-176[»]
2EIPX-ray2.20A/B2-176[»]
4UM4X-ray2.65A/B/C1-176[»]
ProteinModelPortaliP0A7A9.
SMRiP0A7A9. Positions 2-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259312. 36 interactions.
DIPiDIP-36217N.
IntActiP0A7A9. 36 interactions.
MINTiMINT-1226708.
STRINGi511145.b4226.

2D gel databases

SWISS-2DPAGEP0A7A9.

Proteomic databases

EPDiP0A7A9.
PaxDbiP0A7A9.
PRIDEiP0A7A9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77183; AAC77183; b4226.
BAE78227; BAE78227; BAE78227.
GeneIDi948748.
KEGGiecj:JW4185.
eco:b4226.
PATRICi32124027. VBIEscCol129921_4358.

Organism-specific databases

EchoBASEiEB0748.
EcoGeneiEG10755. ppa.

Phylogenomic databases

eggNOGiENOG4105F0N. Bacteria.
COG0221. LUCA.
HOGENOMiHOG000236473.
InParanoidiP0A7A9.
KOiK01507.
OMAiPVALMKM.
OrthoDBiEOG6NKR4X.
PhylomeDBiP0A7A9.

Enzyme and pathway databases

BioCyciEcoCyc:INORGPYROPHOSPHAT-MONOMER.
ECOL316407:JW4185-MONOMER.
MetaCyc:INORGPYROPHOSPHAT-MONOMER.
BRENDAi3.6.1.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A7A9.
PROiP0A7A9.

Family and domain databases

Gene3Di3.90.80.10. 1 hit.
HAMAPiMF_00209. Inorganic_PPase.
InterProiIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERiPTHR10286. PTHR10286. 1 hit.
PfamiPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF50324. SSF50324. 1 hit.
PROSITEiPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12."
    Lahti R., Pitkaeranta T., Valve E., Ilta I., Kukko-Kalske E., Heinonen J.
    J. Bacteriol. 170:5901-5907(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21 AND 95-106.
    Strain: K12 / EMG2.
  6. "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 YEAST AND K.LACTIS PPASES.
  7. "A site-directed mutagenesis study on Escherichia coli inorganic pyrophosphatase. Glutamic acid-98 and lysine-104 are important for structural integrity, whereas aspartic acids-97 and -102 are essential for catalytic activity."
    Lahti R., Pohjanoksa K., Pitkaeranta T., Heikinheimo P., Salminen T., Meyer P., Heinonen J.
    Biochemistry 29:5761-5766(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  8. "Genetic engineering of Escherichia coli inorganic pyrophosphatase. Tyr55 and Tyr141 are important for the structural integrity."
    Lahti R., Salminen T., Latonen S., Heikinheimo P., Pohjanoksa K., Heinonen J.
    Eur. J. Biochem. 198:293-297(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYROSINE RESIDUES.
  9. "Modification of tryptophan 149 of inorganic pyrophosphatase from Escherichia coli."
    Kaneko S., Ichiba T., Hirano N., Hachimori A.
    Int. J. Biochem. 25:233-238(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INACTIVATION.
  10. "The structure of E.coli soluble inorganic pyrophosphatase at 2.7-A resolution."
    Kankare J., Neal G.S., Salminen T., Glumhoff T., Cooperman B.S., Lahti R., Goldman A.
    Protein Eng. 7:823-830(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  11. Erratum
    Kankare J., Neal G.S., Salminen T., Glumhoff T., Cooperman B.S., Lahti R., Goldman A.
    Protein Eng. 7:1173-1173(1994)
  12. "Crystallographic identification of metal-binding sites in Escherichia coli inorganic pyrophosphatase."
    Kankare J., Salminen T., Lahti R., Cooperman B.S., Baykov A.A., Goldman A.
    Biochemistry 35:4670-4677(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  13. "Sructure of Escherichia coli inorganic pyrophosphatase at 2.2-A resolution."
    Kankare J., Salminen T., Lahti R., Cooperman B.S., Baykov A.A., Goldman A.
    Acta Crystallogr. D 52:551-563(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  14. "Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO4(2-). Ligand-induced molecular asymmetry."
    Avaeva S., Kurilova S., Nazarova T., Rodina E., Vorobyeva N., Sklyankina V., Grigorjeva O., Harutyunyan E., Oganessyan V., Wilson K., Dauter Z., Huber R., Mather T.
    FEBS Lett. 410:502-508(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  15. "Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis."
    Harutyunyan E.H., Oganessyan V.Y., Oganessyan N.N., Avaeva S.M., Nazarova T.I., Vorobyeva N.N., Kurilova S.A., Huber R., Mather T.
    Biochemistry 36:7754-7760(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiIPYR_ECOLI
AccessioniPrimary (citable) accession number: P0A7A9
Secondary accession number(s): P17288, Q2M679
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.