Reviewed, UniProtKB/Swiss-Prot P0A7A9 (IPYR_ECOLI)

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:	ppa
Ordered Locus Names:	b4226, JW4185

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	176 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 + H2O = 2 phosphate. HAMAP MF_00209
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. HAMAP MF_00209
Subunit structure	Homohexamer. HAMAP MF_00209
Subcellular location	Cytoplasm HAMAP MF_00209.
Sequence similarities	Belongs to the PPase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
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 Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	inorganic diphosphatase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 176

175

Inorganic pyrophosphatase HAMAP MF_00209

PRO_0000137495

Sites

Metal binding

66

1

Magnesium 1 HAMAP MF_00209

Metal binding

71

1

Magnesium 1 HAMAP MF_00209

Metal binding

71

1

Magnesium 2 HAMAP MF_00209

Metal binding

103

1

Magnesium 1 HAMAP MF_00209

Experimental info

Mutagenesis

21

1

E → D: 16% activity. Ref.8

Mutagenesis

30

1

K → R: 2% activity. Ref.8

Mutagenesis

32

1

E → D: 6% activity. Ref.8

Mutagenesis

44

1

R → K: 10% activity. Ref.8

Mutagenesis

52

1

Y → F: 64% activity. Ref.8

Mutagenesis

56

1

Y → F: 7% activity. Ref.8

Mutagenesis

66

1

D → E: 6% activity. Ref.8

Mutagenesis

68

1

D → E: 1% activity. Ref.8

Mutagenesis

71

1

D → E: No activity. Ref.8

Mutagenesis

98

1

D → E: 22% activity. Ref.8

Mutagenesis

98

1

D → V: No activity. Ref.8

Mutagenesis

99

1

E → V: 33% activity. Ref.8

Mutagenesis

103

1

D → E: 3% activity. Ref.8

Mutagenesis

103

1

D → V: No activity. Ref.8

Mutagenesis

105

1

K → I: No activity. Ref.8

Mutagenesis

105

1

K → R: 3% activity. Ref.8

Mutagenesis

142

1

Y → F: 22% activity. Ref.8

Secondary structure

1

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176

Helix Strand Turn

Details...

Helix

3 – 5

3

Turn

12 – 14

3

Beta strand

15 – 22

8

Beta strand

28 – 33

6

Turn

35 – 37

3

Beta strand

40 – 45

6

Beta strand

47 – 50

4

Beta strand

53 – 58

6

Beta strand

71 – 74

4

Beta strand

85 – 98

14

Beta strand

101 – 110

10

Turn

112 – 114

3

Turn

117 – 120

4

Helix

124 – 126

3

Helix

129 – 141

13

Turn

142 – 145

4

Beta strand

151 – 157

7

Helix

159 – 175

17

Sequences

	Sequence		Length	Mass (Da)
	P0A7A9-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 4C97E51F3BE650DE	FASTA	176	19,704
	10 20 30 40 50 60 MSLLNVPAGK DLPEDIYVVI EIPANADPIK YEIDKESGAL FVDRFMSTAM FYPCNYGYIN 70 80 90 100 110 120 HTLSLDGDPV DVLVPTPYPL QPGSVIRCRP VGVLKMTDEA GEDAKLVAVP HSKLSKEYDH 130 140 150 160 170 IKDVNDLPEL LKAQIAHFFE HYKDLEKGKW VKVEGWENAE AAKAEIVASF ERAKNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2848015] [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: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 9298646] [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: 2160278] [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: 1974462] [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: 1645654] [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: 8383066] [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: 7971944] [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: 8664256] [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: 15299678] [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: 9237692] [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: 9201917] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M23550 Unassigned DNA. Translation: AAB88583.1.
U14003 Genomic DNA. Translation: AAA97123.1.
U00096 Genomic DNA. Translation: AAC77183.1.
AP009048 Genomic DNA. Translation: BAE78227.1.

PIR

PWEC. A27648.

RefSeq

AP_004726.1.
NP_418647.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FAJ	X-ray	2.15	A	2-176	[»]
1I40	X-ray	1.10	A	2-175	[»]
1I6T	X-ray	1.20	A	2-175	[»]
1IGP	X-ray	2.20	A	2-175	[»]
1INO	X-ray	2.20	A	2-175	[»]
1IPW	X-ray	2.30	A/B	2-176	[»]
1JFD	X-ray	2.20	A/B	2-176	[»]
1MJW	X-ray	1.95	A/B	2-175	[»]
1MJX	X-ray	2.15	A/B	2-175	[»]
1MJY	X-ray	2.10	A/B	2-175	[»]
1MJZ	X-ray	2.20	A	2-175	[»]
1OBW	X-ray	1.90	A/B/C	2-176	[»]
2AU6	X-ray	1.20	A	2-175	[»]
2AU7	X-ray	1.05	A	2-175	[»]
2AU8	X-ray	1.65	A	2-175	[»]
2AU9	X-ray	1.30	A	2-175	[»]
2AUU	X-ray	1.22	A	2-175	[»]
2EIP	X-ray	2.20	A/B	2-176	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A7A9.

PTM databases

PhosSite

P0A7A9.

2-D gel databases

SWISS-2DPAGE

P0A7A9.

2DBase-Ecoli

P0A7A9.

Genome annotation databases

GeneID

948748.

GenomeReviews

Gene locus JW4185 in contig AP009048_GR.
Gene locus b4226 in contig U00096_GR.

KEGG

ecj:JW4185.
eco:b4226.

Organism-specific databases

EchoBASE

EB0748.

EcoGene

EG10755. ppa.

CMR

Search...

Phylogenomic databases

eggNOG

COG0221.

HOGENOM

HBG529150.

OMA

EIDKDTG.

Enzyme and pathway databases

BioCyc

EcoCyc:INORGPYROPHOSPHAT-MONOMER.
ECOL168927:B4226-MONOMER.
MetaCyc:INORGPYROPHOSPHAT-MONOMER.

Gene expression databases

Genevestigator

P0A7A9.

Family and domain databases

HAMAP

MF_00209. Inorganic_PPase.
[Tree]

InterPro

IPR008162. Pyrophosphatase.
[Graphical view]

Gene3D

G3DSA:3.90.80.10. Pyrophosphatase. 1 hit.

PANTHER

PTHR10286. Pyrophosphatase. 1 hit.

Pfam

PF00719. Pyrophosphatase. 1 hit.
[Graphical view]

PROSITE

PS00387. PPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

IPYR_ECOLI

Accession

Primary (citable) accession number: P0A7A9
Secondary accession number(s): P17288, Q2M679

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)