UniProtKB - P25536 (NTPPA_ECOLI)
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>sp|P25536|NTPPA_ECOLI dTTP/UTP pyrophosphatase OS=Escherichia coli (strain K12) OX=83333 GN=yhdE PE=1 SV=1 MTSLYLASGSPRRQELLAQLGVTFERIVTGIEEQRQPQESAQQYVVRLAREKARAGVAQT AKDLPVLGADTIVILNGEVLEKPRDAEHAAQMLRKLSGQTHQVMTAVALADSQHILDCLV VTDVTFRTLTDEDIAGYVASDEPLDKAGAYGIQGLGGCFVRKINGSYHAVVGLPLVETYE LLSNFNALREKRDKHDGCommunity curation ()Add a publicationFeedback
dTTP/UTP pyrophosphatase
yhdE
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153. - Ref.7"A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe."
Shen Q., Tan H., Xing G.W., Zheng J., Jia Z.
Sci. Rep. 7:8169-8169(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-33. - Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- dTTPEC:3.6.1.9
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<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153. - Ref.7"A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe."
Shen Q., Tan H., Xing G.W., Zheng J., Jia Z.
Sci. Rep. 7:8169-8169(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-33. - Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
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Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153. - Ref.7"A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe."
Shen Q., Tan H., Xing G.W., Zheng J., Jia Z.
Sci. Rep. 7:8169-8169(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-33. - Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
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- H2OEC:3.6.1.9
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Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153. - Ref.7"A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe."
Shen Q., Tan H., Xing G.W., Zheng J., Jia Z.
Sci. Rep. 7:8169-8169(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-33. - Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
- Search proteins in UniProtKB for this EC number.
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Manual assertion according to rulesi
3 PublicationsManual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153. - Ref.7"A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe."
Shen Q., Tan H., Xing G.W., Zheng J., Jia Z.
Sci. Rep. 7:8169-8169(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-33. - Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
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H2O- Search proteins in UniProtKB for this molecule.
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=diphosphate- Search proteins in UniProtKB for this molecule.
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- H2O
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Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
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H2O- Search proteins in UniProtKB for this molecule.
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+TTP- Search proteins in UniProtKB for this molecule.
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- H2O
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Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
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H2O- Search proteins in UniProtKB for this molecule.
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- 5-methyl-CTP
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Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
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Manual assertion according to rulesi
1 PublicationManual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153. - Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
- KM=53.0 µM for dTTP1 Publication
Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- KM=0.09 mM for dTTP1 Publication
Manual assertion based on experiment ini
- Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
- KM=69.1 µM for UTP1 Publication
Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- KM=0.5 mM for UTP1 Publication
Manual assertion based on experiment ini
- Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
- KM=105.9 µM for CTP1 Publication
Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- KM=32.0 µM for m5UTP1 Publication
Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- KM=44.8 µM for m5CTP1 Publication
Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- KM=47.2 µM for pseudo-UTP1 Publication
Manual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 12 | Important for substrate specificityUniRule annotation Manual assertion according to rulesi 1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 70 | Proton acceptorUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 | |
Sitei | 71 | Important for substrate specificityUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 | |
Sitei | 153 | Important for substrate specificityUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- dTTP diphosphatase activity Source: EcoCyc
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- manganese ion binding Source: EcoCycInferred from direct assayi
- Ref.7"A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe."
Shen Q., Tan H., Xing G.W., Zheng J., Jia Z.
Sci. Rep. 7:8169-8169(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-33.
- NADH pyrophosphatase activity Source: UniProtKB-EC
- nucleoside-triphosphate diphosphatase activity Source: EcoliWikiInferred from direct assayi
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
- UTP diphosphatase activity Source: EcoCycInferred from direct assayi
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
GO - Biological processi
- nucleotide metabolic process Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Hydrolase |
Biological process | Nucleotide metabolism |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11298-MONOMER MetaCyc:EG11298-MONOMER |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: dTTP/UTP pyrophosphataseUniRule annotationManual assertion according to rulesi Curated (EC:3.6.1.9
Manual assertion according to rulesi 3 PublicationsManual assertion based on experiment ini
Short name: dTTPase/UTPase1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini Manual assertion according to rulesi Alternative name(s): Nucleoside triphosphate pyrophosphatase1 Publication Manual assertion based on opinion ini
Manual assertion according to rulesi Nucleotide pyrophosphatase1 Publication Manual assertion based on opinion ini
Manual assertion according to rulesi Short name: Nucleotide PPase1 Publication Manual assertion based on opinion ini
Manual assertion according to rulesi |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:yhdE Ordered Locus Names:b3248, JW3217 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cytoplasm UniRule annotation
Manual assertion according to rulesi
Curated
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cytoplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Manual assertion based on experiment ini
- Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 8 | S → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 10 | S → A: Decrease in activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 12 | R → A: Slight decrease in activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 13 | R → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 32 | E → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 33 | E → A: Loss of activity. Has weak pyrophosphatase activity when assayed using PPi fluorescence sensor. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 52 | K → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 70 | D → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 81 | E → A: Strong decrease in activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 82 | K → A: Strong decrease in activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 150 | Y → A: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 153 | Q → A: Strong decrease in activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 153 | Q → E: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000122981 | 1 – 197 | dTTP/UTP pyrophosphataseAdd BLAST | 197 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P25536 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P25536 |
PRoteomics IDEntifications database More...PRIDEi | P25536 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer (PubMed:24210219, PubMed:25658941, PubMed:26252214). Can also form homotetramers (PubMed:24210219).
3 PublicationsManual assertion based on experiment ini
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153. - Ref.8"Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli."
Jin J., Wu R., Zhu J., Yang S., Lei Z., Wang N., Singh V.K., Zheng J., Jia Z.
PLoS ONE 10:E0117823-E0117823(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-190 OF MUTANT ALA-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISRUPTION PHENOTYPE.
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4262448, 147 interactors 852065, 1 interactor |
Protein interaction database and analysis system More...IntActi | P25536, 4 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b3248 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 4 – 6 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 11 – 19 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 24 – 26 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 41 – 58 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
Beta strandi | 66 – 75 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 78 – 80 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 86 – 96 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 100 – 110 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 115 – 126 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Helixi | 131 – 138 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 142 – 145 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 147 – 149 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 152 – 154 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 155 – 159 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 160 – 165 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 167 – 171 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 175 – 188 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P25536 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Manual assertion according to rulesi
1 PublicationManual assertion inferred by curator fromi
- Ref.5"Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides."
Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X., Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N., Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G., Yakunin A.F.
Chem. Biol. 20:1386-1398(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-8; SER-10; ARG-12; ARG-13; GLU-32; GLU-33; LYS-52; ASP-70; GLU-81; LYS-82; TYR-150 AND GLN-153.
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0424, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_040416_2_1_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P25536 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P25536 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00555, Maf, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.90.950.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00528, Maf, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029001, ITPase-like_fam IPR003697, Maf-like |
The PANTHER Classification System More...PANTHERi | PTHR43213, PTHR43213, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02545, Maf, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF006305, Maf, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52972, SSF52972, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00172, maf, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
10 20 30 40 50
MTSLYLASGS PRRQELLAQL GVTFERIVTG IEEQRQPQES AQQYVVRLAR
60 70 80 90 100
EKARAGVAQT AKDLPVLGAD TIVILNGEVL EKPRDAEHAA QMLRKLSGQT
110 120 130 140 150
HQVMTAVALA DSQHILDCLV VTDVTFRTLT DEDIAGYVAS DEPLDKAGAY
160 170 180 190
GIQGLGGCFV RKINGSYHAV VGLPLVETYE LLSNFNALRE KRDKHDG
<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X57166 Genomic DNA Translation: CAA40456.1 U18997 Genomic DNA Translation: AAA58051.1 Different initiation. U00096 Genomic DNA Translation: AAC76280.1 AP009048 Genomic DNA Translation: BAE77290.1 |
Protein sequence database of the Protein Information Resource More...PIRi | JQ1271 |
NCBI Reference Sequences More...RefSeqi | NP_417714.1, NC_000913.3 WP_000203105.1, NZ_SSZK01000034.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76280; AAC76280; b3248 BAE77290; BAE77290; BAE77290 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947753 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3217 eco:b3248 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3481 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P25536 | dTTP/UTP pyrophosphatase | 217 | UniRef100_P25536 | |||
dTTP/UTP pyrophosphatase | 217 | |||||
Nucleoside triphosphate pyrophosphatase YhdE (Fragment) | 186 | |||||
Nucleoside triphosphate pyrophosphatase YhdE | 197 | |||||
dTTP/UTP pyrophosphatase | 197 | |||||
+22 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P25536 | dTTP/UTP pyrophosphatase | 197 | UniRef90_P25536 | |||
dTTP/UTP pyrophosphatase | 197 | |||||
dTTP/UTP pyrophosphatase | 197 | |||||
dTTP/UTP pyrophosphatase | 197 | |||||
dTTP/UTP pyrophosphatase | 197 | |||||
+463 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P25536 | dTTP/UTP pyrophosphatase | 197 | UniRef50_P25536 | |||
dTTP/UTP pyrophosphatase | 197 | |||||
dTTP/UTP pyrophosphatase | 197 | |||||
Nucleoside triphosphate pyrophosphatase | 197 | |||||
dTTP/UTP pyrophosphatase | 197 | |||||
+1173 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X57166 Genomic DNA Translation: CAA40456.1 U18997 Genomic DNA Translation: AAA58051.1 Different initiation. U00096 Genomic DNA Translation: AAC76280.1 AP009048 Genomic DNA Translation: BAE77290.1 |
PIRi | JQ1271 |
RefSeqi | NP_417714.1, NC_000913.3 WP_000203105.1, NZ_SSZK01000034.1 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4P0E | X-ray | 2.30 | A/B | 2-190 | [»] | |
SMRi | P25536 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262448, 147 interactors 852065, 1 interactor |
IntActi | P25536, 4 interactors |
STRINGi | 511145.b3248 |
Proteomic databases
jPOSTi | P25536 |
PaxDbi | P25536 |
PRIDEi | P25536 |
Genome annotation databases
EnsemblBacteriai | AAC76280; AAC76280; b3248 BAE77290; BAE77290; BAE77290 |
GeneIDi | 947753 |
KEGGi | ecj:JW3217 eco:b3248 |
PATRICi | fig|1411691.4.peg.3481 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1275 |
Phylogenomic databases
eggNOGi | COG0424, Bacteria |
HOGENOMi | CLU_040416_2_1_6 |
InParanoidi | P25536 |
PhylomeDBi | P25536 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG11298-MONOMER MetaCyc:EG11298-MONOMER |
Miscellaneous databases
Protein Ontology More...PROi | PR:P25536 |
Family and domain databases
CDDi | cd00555, Maf, 1 hit |
Gene3Di | 3.90.950.10, 1 hit |
HAMAPi | MF_00528, Maf, 1 hit |
InterProi | View protein in InterPro IPR029001, ITPase-like_fam IPR003697, Maf-like |
PANTHERi | PTHR43213, PTHR43213, 1 hit |
Pfami | View protein in Pfam PF02545, Maf, 1 hit |
PIRSFi | PIRSF006305, Maf, 1 hit |
SUPFAMi | SSF52972, SSF52972, 1 hit |
TIGRFAMsi | TIGR00172, maf, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | NTPPA_ECOLI | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P25536Primary (citable) accession number: P25536 Secondary accession number(s): Q2M8W6 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | May 1, 1992 | |
Last modified: | February 10, 2021 | |
This is version 137 of the entry and version 1 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families