IPYR_ECOLI
ID IPYR_ECOLI Reviewed; 176 AA.
AC P0A7A9; P17288; Q2M679;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00209};
DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00209};
DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00209};
DE Short=PPase {ECO:0000255|HAMAP-Rule:MF_00209};
GN Name=ppa {ECO:0000255|HAMAP-Rule:MF_00209};
GN OrderedLocusNames=b4226, JW4185;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2848015; DOI=10.1128/jb.170.12.5901-5907.1988;
RA Lahti R., Pitkaeranta T., Valve E., Ilta I., Kukko-Kalske E., Heinonen J.;
RT "Cloning and characterization of the gene encoding inorganic
RT pyrophosphatase of Escherichia coli K-12.";
RL J. Bacteriol. 170:5901-5907(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-21 AND 95-106.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP SIMILARITY TO YEAST AND K.LACTIS PPASES.
RX PubMed=2160278; DOI=10.1016/0167-4838(90)90246-c;
RA Lahti R., Kolakowski L.F. Jr., Heinonen J., Vihinen M., Pohjanoksa K.,
RA Cooperman B.S.;
RT "Conservation of functional residues between yeast and E. coli inorganic
RT pyrophosphatases.";
RL Biochim. Biophys. Acta 1038:338-345(1990).
RN [7]
RP MUTAGENESIS.
RX PubMed=1974462; DOI=10.1021/bi00476a017;
RA Lahti R., Pohjanoksa K., Pitkaeranta T., Heikinheimo P., Salminen T.,
RA Meyer P., Heinonen J.;
RT "A site-directed mutagenesis study on Escherichia coli inorganic
RT pyrophosphatase. Glutamic acid-98 and lysine-104 are important for
RT structural integrity, whereas aspartic acids-97 and -102 are essential for
RT catalytic activity.";
RL Biochemistry 29:5761-5766(1990).
RN [8]
RP MUTAGENESIS OF TYROSINE RESIDUES.
RX PubMed=1645654; DOI=10.1111/j.1432-1033.1991.tb16015.x;
RA Lahti R., Salminen T., Latonen S., Heikinheimo P., Pohjanoksa K.,
RA Heinonen J.;
RT "Genetic engineering of Escherichia coli inorganic pyrophosphatase. Tyr55
RT and Tyr141 are important for the structural integrity.";
RL Eur. J. Biochem. 198:293-297(1991).
RN [9]
RP INACTIVATION.
RX PubMed=8383066; DOI=10.1016/0020-711x(93)90011-3;
RA Kaneko S., Ichiba T., Hirano N., Hachimori A.;
RT "Modification of tryptophan 149 of inorganic pyrophosphatase from
RT Escherichia coli.";
RL Int. J. Biochem. 25:233-238(1993).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=7971944; DOI=10.1093/protein/7.7.823;
RA Kankare J., Neal G.S., Salminen T., Glumhoff T., Cooperman B.S., Lahti R.,
RA Goldman A.;
RT "The structure of E.coli soluble inorganic pyrophosphatase at 2.7-A
RT resolution.";
RL Protein Eng. 7:823-830(1994).
RN [11]
RP ERRATUM OF PUBMED:7971944.
RA Kankare J., Neal G.S., Salminen T., Glumhoff T., Cooperman B.S., Lahti R.,
RA Goldman A.;
RL Protein Eng. 7:1173-1173(1994).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=8664256; DOI=10.1021/bi952637e;
RA Kankare J., Salminen T., Lahti R., Cooperman B.S., Baykov A.A., Goldman A.;
RT "Crystallographic identification of metal-binding sites in Escherichia coli
RT inorganic pyrophosphatase.";
RL Biochemistry 35:4670-4677(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=15299678; DOI=10.1107/s0907444996000376;
RA Kankare J., Salminen T., Lahti R., Cooperman B.S., Baykov A.A., Goldman A.;
RT "Sructure of Escherichia coli inorganic pyrophosphatase at 2.2-A
RT resolution.";
RL Acta Crystallogr. D 52:551-563(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX PubMed=9237692; DOI=10.1016/s0014-5793(97)00650-9;
RA Avaeva S., Kurilova S., Nazarova T., Rodina E., Vorobyeva N.,
RA Sklyankina V., Grigorjeva O., Harutyunyan E., Oganessyan V., Wilson K.,
RA Dauter Z., Huber R., Mather T.;
RT "Crystal structure of Escherichia coli inorganic pyrophosphatase complexed
RT with SO4(2-). Ligand-induced molecular asymmetry.";
RL FEBS Lett. 410:502-508(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9201917; DOI=10.1021/bi962637u;
RA Harutyunyan E.H., Oganessyan V.Y., Oganessyan N.N., Avaeva S.M.,
RA Nazarova T.I., Vorobyeva N.N., Kurilova S.A., Huber R., Mather T.;
RT "Crystal structure of holo inorganic pyrophosphatase from Escherichia coli
RT at 1.9 A resolution. Mechanism of hydrolysis.";
RL Biochemistry 36:7754-7760(1997).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00209};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00209};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00209}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00209}.
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DR EMBL; M23550; AAB88583.1; -; Unassigned_DNA.
DR EMBL; U14003; AAA97123.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77183.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78227.1; -; Genomic_DNA.
DR PIR; A27648; PWEC.
DR RefSeq; NP_418647.1; NC_000913.3.
DR RefSeq; WP_000055075.1; NZ_SSUV01000014.1.
DR PDB; 1FAJ; X-ray; 2.15 A; A=2-176.
DR PDB; 1I40; X-ray; 1.10 A; A=2-176.
DR PDB; 1I6T; X-ray; 1.20 A; A=2-176.
DR PDB; 1IGP; X-ray; 2.20 A; A=2-176.
DR PDB; 1INO; X-ray; 2.20 A; A=2-176.
DR PDB; 1IPW; X-ray; 2.30 A; A/B=2-176.
DR PDB; 1JFD; X-ray; 2.20 A; A/B=2-176.
DR PDB; 1MJW; X-ray; 1.95 A; A/B=2-176.
DR PDB; 1MJX; X-ray; 2.15 A; A/B=2-176.
DR PDB; 1MJY; X-ray; 2.10 A; A/B=2-176.
DR PDB; 1MJZ; X-ray; 2.20 A; A=2-176.
DR PDB; 1OBW; X-ray; 1.90 A; A/B/C=2-176.
DR PDB; 2AU6; X-ray; 1.20 A; A=2-176.
DR PDB; 2AU7; X-ray; 1.05 A; A=2-176.
DR PDB; 2AU8; X-ray; 1.65 A; A=2-176.
DR PDB; 2AU9; X-ray; 1.30 A; A=2-176.
DR PDB; 2AUU; X-ray; 1.22 A; A=2-176.
DR PDB; 2EIP; X-ray; 2.20 A; A/B=2-176.
DR PDB; 4UM4; X-ray; 2.65 A; A/B/C=1-176.
DR PDBsum; 1FAJ; -.
DR PDBsum; 1I40; -.
DR PDBsum; 1I6T; -.
DR PDBsum; 1IGP; -.
DR PDBsum; 1INO; -.
DR PDBsum; 1IPW; -.
DR PDBsum; 1JFD; -.
DR PDBsum; 1MJW; -.
DR PDBsum; 1MJX; -.
DR PDBsum; 1MJY; -.
DR PDBsum; 1MJZ; -.
DR PDBsum; 1OBW; -.
DR PDBsum; 2AU6; -.
DR PDBsum; 2AU7; -.
DR PDBsum; 2AU8; -.
DR PDBsum; 2AU9; -.
DR PDBsum; 2AUU; -.
DR PDBsum; 2EIP; -.
DR PDBsum; 4UM4; -.
DR AlphaFoldDB; P0A7A9; -.
DR SASBDB; P0A7A9; -.
DR SMR; P0A7A9; -.
DR BioGRID; 4259312; 48.
DR DIP; DIP-36217N; -.
DR IntAct; P0A7A9; 37.
DR STRING; 511145.b4226; -.
DR BindingDB; P0A7A9; -.
DR SWISS-2DPAGE; P0A7A9; -.
DR jPOST; P0A7A9; -.
DR PaxDb; P0A7A9; -.
DR PRIDE; P0A7A9; -.
DR EnsemblBacteria; AAC77183; AAC77183; b4226.
DR EnsemblBacteria; BAE78227; BAE78227; BAE78227.
DR GeneID; 948748; -.
DR KEGG; ecj:JW4185; -.
DR KEGG; eco:b4226; -.
DR PATRIC; fig|1411691.4.peg.2475; -.
DR EchoBASE; EB0748; -.
DR eggNOG; COG0221; Bacteria.
DR HOGENOM; CLU_073198_1_0_6; -.
DR InParanoid; P0A7A9; -.
DR OMA; DEPTFPG; -.
DR PhylomeDB; P0A7A9; -.
DR BioCyc; EcoCyc:INORGPYROPHOSPHAT-MON; -.
DR BioCyc; MetaCyc:INORGPYROPHOSPHAT-MON; -.
DR BRENDA; 3.6.1.1; 2026.
DR EvolutionaryTrace; P0A7A9; -.
DR PRO; PR:P0A7A9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0050355; F:triphosphatase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 3.90.80.10; -; 1.
DR HAMAP; MF_00209; Inorganic_PPase; 1.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; SSF50324; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..176
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137495"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT MUTAGEN 21
FT /note="E->D: 16% activity."
FT MUTAGEN 30
FT /note="K->R: 2% activity."
FT MUTAGEN 32
FT /note="E->D: 6% activity."
FT MUTAGEN 44
FT /note="R->K: 10% activity."
FT MUTAGEN 52
FT /note="Y->F: 64% activity."
FT MUTAGEN 56
FT /note="Y->F: 7% activity."
FT MUTAGEN 66
FT /note="D->E: 6% activity."
FT MUTAGEN 68
FT /note="D->E: 1% activity."
FT MUTAGEN 71
FT /note="D->E: No activity."
FT MUTAGEN 98
FT /note="D->E: 22% activity."
FT MUTAGEN 98
FT /note="D->V: No activity."
FT MUTAGEN 99
FT /note="E->V: 33% activity."
FT MUTAGEN 103
FT /note="D->E: 3% activity."
FT MUTAGEN 103
FT /note="D->V: No activity."
FT MUTAGEN 105
FT /note="K->I: No activity."
FT MUTAGEN 105
FT /note="K->R: 3% activity."
FT MUTAGEN 142
FT /note="Y->F: 22% activity."
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1IGP"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2AU7"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1INO"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 85..98
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1IGP"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2AU7"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2AU7"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2AU7"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2AU7"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:2AU7"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:2AU7"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2AU7"
FT HELIX 159..175
FT /evidence="ECO:0007829|PDB:2AU7"
SQ SEQUENCE 176 AA; 19704 MW; 4C97E51F3BE650DE CRC64;
MSLLNVPAGK DLPEDIYVVI EIPANADPIK YEIDKESGAL FVDRFMSTAM FYPCNYGYIN
HTLSLDGDPV DVLVPTPYPL QPGSVIRCRP VGVLKMTDEA GEDAKLVAVP HSKLSKEYDH
IKDVNDLPEL LKAQIAHFFE HYKDLEKGKW VKVEGWENAE AAKAEIVASF ERAKNK