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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
 
 
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