UniProtKB - P07379 (PCKGC_RAT)
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>sp|P07379|PCKGC_RAT Phosphoenolpyruvate carboxykinase, cytosolic [GTP] OS=Rattus norvegicus OX=10116 GN=Pck1 PE=1 SV=1 MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHM QEEGVIRKLKKYDNCWLALTDPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEE DFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIELTDSPYVVASMRIMTRMGTSV LEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTL PGWKVECVGDDIAWMKFDAQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNV AETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCAHPNSRFCTPASQCPIIDPAW ESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWM FGRIEGEDSAKLTPIGYVPKEDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQV NADLPYEIERELRALKQRISQMCommunity curation ()Add a publicationFeedback
Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Pck1
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 which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
6 Publications<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.4"Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase."
Ballard F.J., Hanson R.W.
J. Biol. Chem. 244:5625-5630(1969) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.17"Asymmetric anchoring is required for efficient omega-loop opening and closing in cytosolic phosphoenolpyruvate carboxykinase."
Cui D.S., Broom A., Mcleod M.J., Meiering E.M., Holyoak T.
Biochemistry 56:2106-2115(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, MUTAGENESIS OF HIS-477. - Ref.18"Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel inhibitor of phosphoenolpyruvate carboxykinase."
Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.
Biochemistry 58:3918-3926(2019) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
Miscellaneous
<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
- GTPEC:4.1.1.32
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Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.17"Asymmetric anchoring is required for efficient omega-loop opening and closing in cytosolic phosphoenolpyruvate carboxykinase."
Cui D.S., Broom A., Mcleod M.J., Meiering E.M., Holyoak T.
Biochemistry 56:2106-2115(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, MUTAGENESIS OF HIS-477. - Ref.18"Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel inhibitor of phosphoenolpyruvate carboxykinase."
Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.
Biochemistry 58:3918-3926(2019) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
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Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.17"Asymmetric anchoring is required for efficient omega-loop opening and closing in cytosolic phosphoenolpyruvate carboxykinase."
Cui D.S., Broom A., Mcleod M.J., Meiering E.M., Holyoak T.
Biochemistry 56:2106-2115(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, MUTAGENESIS OF HIS-477. - Ref.18"Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel inhibitor of phosphoenolpyruvate carboxykinase."
Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.
Biochemistry 58:3918-3926(2019) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION.
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- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.17"Asymmetric anchoring is required for efficient omega-loop opening and closing in cytosolic phosphoenolpyruvate carboxykinase."
Cui D.S., Broom A., Mcleod M.J., Meiering E.M., Holyoak T.
Biochemistry 56:2106-2115(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, MUTAGENESIS OF HIS-477.
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GTP- Search proteins in UniProtKB for this molecule.
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+oxaloacetate- Search proteins in UniProtKB for this molecule.
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+phosphoenolpyruvate- Search proteins in UniProtKB for this molecule.
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- GTP
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
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GTP- Search proteins in UniProtKB for this molecule.
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+L-seryl-[protein]- Search proteins in UniProtKB for this molecule.
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L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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=GDP- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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O-phospho-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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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 based on experiment ini
- Ref.9"Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid."
Sullivan S.M., Holyoak T.
Biochemistry 46:10078-10088(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.10"Differential inhibition of cytosolic PEPCK by substrate analogues. Kinetic and structural characterization of inhibitor recognition."
Stiffin R.M., Sullivan S.M., Carlson G.M., Holyoak T.
Biochemistry 47:2099-2109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH MANGANESE AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT. - Ref.11"Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection."
Sullivan S.M., Holyoak T.
Proc. Natl. Acad. Sci. U.S.A. 105:13829-13834(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.12"Increasing the conformational entropy of the Omega-loop lid domain in phosphoenolpyruvate carboxykinase impairs catalysis and decreases catalytic fidelity."
Johnson T.A., Holyoak T.
Biochemistry 49:5176-5187(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATES, COFACTOR, SUBUNIT. - Ref.13"The Omega-loop lid domain of phosphoenolpyruvate carboxykinase is essential for catalytic function."
Johnson T.A., Holyoak T.
Biochemistry 51:9547-9559(2012) [PubMed] [Europe PMC] [Abstract] - Ref.14"Three rare diseases in one sib pair: RAI1, PCK1, GRIN2B mutations associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA receptor glutamate insensitivity."
Adams D.R., Yuan H., Holyoak T., Arajs K.H., Hakimi P., Markello T.C., Wolfe L.A., Vilboux T., Burton B.K., Fajardo K.F., Grahame G., Holloman C., Sincan M., Smith A.C., Wells G.A., Huang Y., Vega H., Snyder J.P. , Golas G.A., Tifft C.J., Boerkoel C.F., Hanson R.W., Traynelis S.F., Kerr D.S., Gahl W.A.
Mol. Genet. Metab. 113:161-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.17"Asymmetric anchoring is required for efficient omega-loop opening and closing in cytosolic phosphoenolpyruvate carboxykinase."
Cui D.S., Broom A., Mcleod M.J., Meiering E.M., Holyoak T.
Biochemistry 56:2106-2115(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, MUTAGENESIS OF HIS-477.
Manual assertion based on experiment ini
- Ref.9"Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid."
Sullivan S.M., Holyoak T.
Biochemistry 46:10078-10088(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.10"Differential inhibition of cytosolic PEPCK by substrate analogues. Kinetic and structural characterization of inhibitor recognition."
Stiffin R.M., Sullivan S.M., Carlson G.M., Holyoak T.
Biochemistry 47:2099-2109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH MANGANESE AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT. - Ref.11"Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection."
Sullivan S.M., Holyoak T.
Proc. Natl. Acad. Sci. U.S.A. 105:13829-13834(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.12"Increasing the conformational entropy of the Omega-loop lid domain in phosphoenolpyruvate carboxykinase impairs catalysis and decreases catalytic fidelity."
Johnson T.A., Holyoak T.
Biochemistry 49:5176-5187(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATES, COFACTOR, SUBUNIT. - Ref.13"The Omega-loop lid domain of phosphoenolpyruvate carboxykinase is essential for catalytic function."
Johnson T.A., Holyoak T.
Biochemistry 51:9547-9559(2012) [PubMed] [Europe PMC] [Abstract] - Ref.14"Three rare diseases in one sib pair: RAI1, PCK1, GRIN2B mutations associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA receptor glutamate insensitivity."
Adams D.R., Yuan H., Holyoak T., Arajs K.H., Hakimi P., Markello T.C., Wolfe L.A., Vilboux T., Burton B.K., Fajardo K.F., Grahame G., Holloman C., Sincan M., Smith A.C., Wells G.A., Huang Y., Vega H., Snyder J.P. , Golas G.A., Tifft C.J., Boerkoel C.F., Hanson R.W., Traynelis S.F., Kerr D.S., Gahl W.A.
Mol. Genet. Metab. 113:161-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.17"Asymmetric anchoring is required for efficient omega-loop opening and closing in cytosolic phosphoenolpyruvate carboxykinase."
Cui D.S., Broom A., Mcleod M.J., Meiering E.M., Holyoak T.
Biochemistry 56:2106-2115(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, MUTAGENESIS OF HIS-477.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Manual assertion inferred from sequence similarity toi
3 PublicationsManual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.18"Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel inhibitor of phosphoenolpyruvate carboxykinase."
Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.
Biochemistry 58:3918-3926(2019) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
<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.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89.
- KM=39 µM for oxaloacetate1 Publication
Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
- KM=161 µM for GTP1 Publication
Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
- KM=301 µM for phosphoenolpyruvate1 Publication
Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
- KM=79 µM for GDP1 Publication
Manual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
- KM=475 µM for phosphoenolpyruvate (for phosphoenolpyruvate carboxykinase in the backward reaction)1 Publication
Manual assertion based on experiment ini
- Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89.
- KM=207 µM for GDP (for phosphoenolpyruvate carboxykinase in the backward reaction)1 Publication
Manual assertion based on experiment ini
- Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89.
- KM=435 µM for CO2 (for phosphoenolpyruvate carboxykinase in the backward reaction)1 Publication
Manual assertion based on experiment ini
- Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89.
- KM=51 µM for oxaloacetate (for phosphoenolpyruvate carboxykinase in the forward reaction)1 Publication
Manual assertion based on experiment ini
- Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89.
- KM=55 µM for GTP (for phosphoenolpyruvate carboxykinase in the forward reaction)1 Publication
Manual assertion based on experiment ini
- Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: gluconeogenesis
This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.1 PublicationManual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 87 | Substrate5 Publications Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 244 | ManganeseCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 10 PublicationsManual assertion based on experiment ini
| 1 | |
Metal bindingi | 264 | Manganese; via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 10 PublicationsManual assertion based on experiment ini
| 1 | |
Binding sitei | 286 | Substrate6 Publications Manual assertion based on experiment ini
| 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 | 288 | 2 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 311 | ManganeseCombined sources Manual assertion inferred from combination of experimental and computational evidencei 10 PublicationsManual assertion based on experiment ini
| 1 | |
Binding sitei | 405 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 7 PublicationsManual assertion based on experiment ini
| 1 | |
Binding sitei | 436 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 8 PublicationsManual assertion based on experiment ini
| 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 287 – 292 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 8 PublicationsManual assertion based on experiment ini
| 6 | |
Nucleotide bindingi | 530 – 533 | GTPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 8 PublicationsManual assertion based on experiment ini
| 4 |
<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
- carboxylic acid binding Source: BHF-UCL
<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.9"Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid."
Sullivan S.M., Holyoak T.
Biochemistry 46:10078-10088(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM.
- GDP binding Source: RGDInferred from direct assayi
- "Response of glucose metabolism enzymes in an acute porphyria model. Role of reactive oxygen species."
Lelli S.M., San Martin de Viale L.C., Mazzetti M.B.
Toxicology 216:49-58(2005) [PubMed] [Europe PMC] [Abstract]
- GTP binding Source: BHF-UCLInferred from direct assayi
- Ref.9"Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid."
Sullivan S.M., Holyoak T.
Biochemistry 46:10078-10088(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM.
- magnesium ion binding Source: BHF-UCL
<p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iss">GO evidence code guide</a></p>
Inferred from sequence or structural similarityi
- "Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site."
Dunten P., Belunis C., Crowther R., Hollfelder K., Kammlott U., Levin W., Michel H., Ramsey G.B., Swain A., Weber D., Wertheimer S.J.
J. Mol. Biol. 316:257-264(2002) [PubMed] [Europe PMC] [Abstract]
- manganese ion binding Source: BHF-UCLInferred from direct assayi
- Ref.9"Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid."
Sullivan S.M., Holyoak T.
Biochemistry 46:10078-10088(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM.
- nucleoside diphosphate kinase activity Source: ReactomeInferred from experimenti
- "Phosphorylation of carbovir enantiomers by cellular enzymes determines the stereoselectivity of antiviral activity."
Miller W.H., Daluge S.M., Garvey E.P., Hopkins S., Reardon J.E., Boyd F.L., Miller R.L.
J Biol Chem 267:21220-21224(1992) [PubMed] [Europe PMC] [Abstract]
- phosphoenolpyruvate carboxykinase (GTP) activity Source: UniProtKBInferred from direct assayi
- Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.18"Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel inhibitor of phosphoenolpyruvate carboxykinase."
Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.
Biochemistry 58:3918-3926(2019) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
- phosphoenolpyruvate carboxykinase activity Source: RGDInferred from direct assayi
- "Mechanism of fat-induced hepatic gluconeogenesis: effect of metformin."
Song S., Andrikopoulos S., Filippis C., Thorburn A.W., Khan D., Proietto J.
Am J Physiol Endocrinol Metab 281:E275-82(2001) [PubMed] [Europe PMC] [Abstract] - "Phosphoenolpyruvate carboxykinase is induced in growth-arrested hepatoma cells."
Zeitouni N., Eubank D.W., Lee A.Q., Oxford M.G., Freeman T.L., Mailliard M.E., Beale E.G.
Biochem Biophys Res Commun 290:1513-1520(2002) [PubMed] [Europe PMC] [Abstract] - "Gluconeogenesis in developing rat kidney cortex."
Zorzoli A., Turkenkopf I.J., Mueller V.L.
Biochem J 111:181-185(1969) [PubMed] [Europe PMC] [Abstract] - "Induction and suppression of the key enzymes of glycolysis and gluconeogenesis in isolated perfused rat liver in response to glucose, fructose and lactate."
Wimhurst J.M., Manchester K.L.
Biochem J 134:143-156(1973) [PubMed] [Europe PMC] [Abstract]
- protein serine kinase activity (using GTP as donor) Source: UniProtKB
GO - Biological processi
- aging Source: RGD
<p>Inferred from Expression Pattern</p>
<p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p>
Inferred from expression patterni
- cellular response to cAMP Source: RGDInferred from expression patterni
- Ref.6"Inhibition of glucagon-signaling and downstream actions by interleukin 1beta and tumor necrosis factor alpha in cultured primary rat hepatocytes."
Christ B.
Horm. Metab. Res. 40:18-23(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
- cellular response to dexamethasone stimulus Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- cellular response to fructose stimulus Source: RGDInferred from expression patterni
- "Fructose induces gluconeogenesis and lipogenesis through a SIRT1-dependent mechanism."
Caton P.W., Nayuni N.K., Khan N.Q., Wood E.G., Corder R.
J Endocrinol 208:273-283(2011) [PubMed] [Europe PMC] [Abstract]
- cellular response to glucagon stimulus Source: RGDInferred from expression patterni
- Ref.6"Inhibition of glucagon-signaling and downstream actions by interleukin 1beta and tumor necrosis factor alpha in cultured primary rat hepatocytes."
Christ B.
Horm. Metab. Res. 40:18-23(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
- cellular response to glucose stimulus Source: UniProtKBInferred from direct assayi
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
- cellular response to hypoxia Source: RGDInferred from expression patterni
- cellular response to insulin stimulus Source: RGDInferred from expression patterni
- "Retinoids induced Pck1 expression and attenuated insulin-mediated suppression of its expression via activation of retinoic acid receptor in primary rat hepatocytes."
Zhang Y., Li R., Chen W., Li Y., Chen G.
Mol Cell Biochem 355:1-8(2011) [PubMed] [Europe PMC] [Abstract]
- cellular response to interleukin-1 Source: RGDInferred from expression patterni
- Ref.6"Inhibition of glucagon-signaling and downstream actions by interleukin 1beta and tumor necrosis factor alpha in cultured primary rat hepatocytes."
Christ B.
Horm. Metab. Res. 40:18-23(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
- cellular response to potassium ion starvation Source: RGD
- cellular response to retinoic acid Source: RGDInferred from expression patterni
- "Retinoids induced Pck1 expression and attenuated insulin-mediated suppression of its expression via activation of retinoic acid receptor in primary rat hepatocytes."
Zhang Y., Li R., Chen W., Li Y., Chen G.
Mol Cell Biochem 355:1-8(2011) [PubMed] [Europe PMC] [Abstract]
- cellular response to tumor necrosis factor Source: RGDInferred from expression patterni
- Ref.6"Inhibition of glucagon-signaling and downstream actions by interleukin 1beta and tumor necrosis factor alpha in cultured primary rat hepatocytes."
Christ B.
Horm. Metab. Res. 40:18-23(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
- gluconeogenesis Source: BHF-UCLInferred from direct assayi
- Ref.4"Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase."
Ballard F.J., Hanson R.W.
J. Biol. Chem. 244:5625-5630(1969) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- glucose homeostasis Source: BHF-UCLInferred from direct assayi
- Ref.4"Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase."
Ballard F.J., Hanson R.W.
J. Biol. Chem. 244:5625-5630(1969) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- glucose metabolic process Source: BHF-UCL
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Efficient delivery of siRNA using dendritic poly(L-lysine) for loss-of-function analysis."
Inoue Y., Kurihara R., Tsuchida A., Hasegawa M., Nagashima T., Mori T., Niidome T., Katayama Y., Okitsu O.
J Control Release 126:59-66(2008) [PubMed] [Europe PMC] [Abstract]
- glycerol biosynthetic process from pyruvate Source: BHF-UCLInferred from direct assayi
- Ref.4"Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase."
Ballard F.J., Hanson R.W.
J. Biol. Chem. 244:5625-5630(1969) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- hepatocyte differentiation Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- lipid metabolic process Source: RGD
- oxaloacetate metabolic process Source: UniProtKBInferred from direct assayi
- Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91. - Ref.18"Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel inhibitor of phosphoenolpyruvate carboxykinase."
Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.
Biochemistry 58:3918-3926(2019) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
- peptidyl-serine phosphorylation Source: UniProtKB
- positive regulation of memory T cell differentiation Source: UniProtKB
- positive regulation of transcription from RNA polymerase II promoter in response to acidic pH Source: RGD
- propionate catabolic process Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- regulation of lipid biosynthetic process Source: UniProtKB
- response to activity Source: RGDInferred from expression patterni
- "Merit of physical exercise to reverse the higher gene expression of hepatic phosphoenolpyruvate carboxykinase in obese Zucker rats."
Chang S.P., Chen Y.H., Chang W.C., Liu I.M., Cheng J.T.
Life Sci 79:240-246(2006) [PubMed] [Europe PMC] [Abstract]
- response to bacterium Source: RGD
- response to insulin Source: BHF-UCLInferred from sequence or structural similarityi
- "Promoter polymorphism in PCK1 (phosphoenolpyruvate carboxykinase gene) associated with type 2 diabetes mellitus."
Cao H., van der Veer E., Ban M.R., Hanley A.J., Zinman B., Harris S.B., Young T.K., Pickering J.G., Hegele R.A.
J Clin Endocrinol Metab 89:898-903(2004) [PubMed] [Europe PMC] [Abstract]
- response to interleukin-6 Source: RGDInferred from expression patterni
- "Impact of interleukin-6 on the glucose metabolic capacity in rat liver."
Lienenluke B., Christ B.
Histochem Cell Biol 128:371-377(2007) [PubMed] [Europe PMC] [Abstract]
- response to lipid Source: RGDInferred from expression patterni
- "Gestational high fat diet programs hepatic phosphoenolpyruvate carboxykinase gene expression and histone modification in neonatal offspring rats."
Strakovsky R.S., Zhang X., Zhou D., Pan Y.X.
J Physiol 589:2707-2717(2011) [PubMed] [Europe PMC] [Abstract]
- response to lipopolysaccharide Source: RGDInferred from expression patterni
- "Endotoxin induced hyperlactatemia and hypoglycemia is linked to decreased mitochondrial phosphoenolpyruvate carboxykinase."
Caton P.W., Nayuni N.K., Murch O., Corder R.
Life Sci 84:738-744(2009) [PubMed] [Europe PMC] [Abstract]
- response to methionine Source: RGDInferred from expression patterni
- "Genomic and metabolic responses to methionine-restricted and methionine-restricted, cysteine-supplemented diets in Fischer 344 rat inguinal adipose tissue, liver and quadriceps muscle."
Perrone C.E., Mattocks D.A., Plummer J.D., Chittur S.V., Mohney R., Vignola K., Orentreich D.S., Orentreich N.
J Nutrigenet Nutrigenomics 5:132-157(2012) [PubMed] [Europe PMC] [Abstract]
- response to starvation Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
<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 | Decarboxylase, Kinase, Lyase, Transferase |
Biological process | Gluconeogenesis |
Ligand | GTP-binding, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 4.1.1.32, 5301 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-RNO-70263, Gluconeogenesis |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P07379 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00138 |
<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: Phosphoenolpyruvate carboxykinase, cytosolic [GTP]Curated (EC:4.1.1.32
Manual assertion based on experiment ini
Short name: PEPCK-C Alternative name(s): Serine-protein kinase PCK1Curated (EC:2.7.11.-
Manual assertion inferred from sequence similarity toi ) |
<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:Pck11 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
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
<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 | Rattus norvegicus (Rat) |
<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 | 10116 [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 › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
<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 |
|
Organism-specific databases
Rat genome database More...RGDi | 3267, Pck1 |
<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
Endoplasmic reticulum
- Endoplasmic reticulum By similarity
Manual assertion inferred from sequence similarity toi
- Endoplasmic reticulum By similarity
Cytoplasm and Cytosol
- cytosol 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
- Ref.4"Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase."
Ballard F.J., Hanson R.W.
J. Biol. Chem. 244:5625-5630(1969) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
Note: Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum.By similarity- cytosol 1 Publication
Manual assertion inferred from sequence similarity toi
Cytosol
- cytosol Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Mitochondrion
- mitochondrion Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- mitochondrion Source: GO_CentralInferred from biological aspect of ancestori
Other locations
- cytoplasm Source: BHF-UCLInferred from direct assayi
- Ref.4"Purification of phosphoenolpyruvate carboxykinase from the cytosol fraction of rat liver and the immunochemical demonstration of differences between this enzyme and the mitochondrial phosphoenolpyruvate carboxykinase."
Ballard F.J., Hanson R.W.
J. Biol. Chem. 244:5625-5630(1969) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- cytoplasm Source: BHF-UCLInferred from direct assayi
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum<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
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 | 89 | E → A, D or Q: Abolished phosphoenolpyruvate carboxykinase activity; decreased affinity for oxaloacetate. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 90 | S → A: Decreased phosphorylation and increased acetylation levels. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 91 | K → Q: 3-fold decrease of affinity for phosphoenolpyruvate. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 477 | H → R: Destabilization of the closed state of the omega-loop, resulting in decreased capture rates for the weaker binding substrates associated with catalysis in the phosphoenolpyruvate to oxaloacetate direction. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL1075234 |
<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_0000103630 | 1 – 622 | Phosphoenolpyruvate carboxykinase, cytosolic [GTP]Add BLAST | 622 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 19 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 70 | N6-acetyllysine; by p300/EP300By similarity Manual assertion inferred from sequence similarity toi | 1 | |
Modified residuei | 71 | N6-acetyllysine; by p300/EP300By similarity Manual assertion inferred from sequence similarity toi | 1 | |
Modified residuei | 90 | PhosphoserineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
Modified residuei | 91 | N6-acetyllysine; by p300/EP300By similarity Manual assertion inferred from sequence similarity toi 1 PublicationManual assertion based on experiment ini
| 1 | |
Modified residuei | 118 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 178 | PhosphothreonineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
Modified residuei | 286 | PhosphoserineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
Modified residuei | 473 | N6-acetyllysine1 Publication Manual assertion based on experiment ini
| 1 | |
Modified residuei | 521 | N6-acetyllysine1 Publication Manual assertion based on experiment ini
| 1 | |
Modified residuei | 524 | N6-acetyllysine1 Publication Manual assertion based on experiment ini
| 1 | |
Modified residuei | 594 | N6-acetyllysine; by p300/EP300By similarity Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Manual assertion inferred from sequence similarity toi
1 PublicationManual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
Manual assertion inferred from sequence similarity toi
1 PublicationManual assertion based on experiment ini
- Ref.8"Dynamic acetylation of phosphoenolpyruvate carboxykinase toggles enzyme activity between gluconeogenic and anaplerotic reactions."
Latorre-Muro P., Baeza J., Armstrong E.A., Hurtado-Guerrero R., Corzana F., Wu L.E., Sinclair D.A., Lopez-Buesa P., Carrodeguas J.A., Denu J.M.
Mol. Cell 71:718-732(2018) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, ACETYLATION AT LYS-91; LYS-473; LYS-521 AND LYS-524, PHOSPHORYLATION, MUTAGENESIS OF SER-90 AND LYS-91.
Manual assertion inferred from sequence similarity toi
Keywords - PTMi
Acetylation, Phosphoprotein, Ubl conjugationProteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P07379 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P07379 |
PRoteomics IDEntifications database More...PRIDEi | P07379 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P07379 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P07379 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Manual assertion based on experiment ini
- Ref.5"Multihormonal regulation of phosphoenolpyruvate carboxykinase gene transcription. The dominant role of insulin."
Sasaki K., Cripe T.P., Koch S.R., Andreone T.L., Petersen D.D., Beale E.G., Granner D.K.
J. Biol. Chem. 259:15242-15251(1984) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION. - Ref.6"Inhibition of glucagon-signaling and downstream actions by interleukin 1beta and tumor necrosis factor alpha in cultured primary rat hepatocytes."
Christ B.
Horm. Metab. Res. 40:18-23(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSRNOG00000028616, Expressed in kidney and 21 other tissues |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P07379, RN |
<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
Monomer.
8 PublicationsManual assertion based on experiment ini
- Ref.9"Structures of rat cytosolic PEPCK: insight into the mechanism of phosphorylation and decarboxylation of oxaloacetic acid."
Sullivan S.M., Holyoak T.
Biochemistry 46:10078-10088(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.10"Differential inhibition of cytosolic PEPCK by substrate analogues. Kinetic and structural characterization of inhibitor recognition."
Stiffin R.M., Sullivan S.M., Carlson G.M., Holyoak T.
Biochemistry 47:2099-2109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH MANGANESE AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT. - Ref.11"Enzymes with lid-gated active sites must operate by an induced fit mechanism instead of conformational selection."
Sullivan S.M., Holyoak T.
Proc. Natl. Acad. Sci. U.S.A. 105:13829-13834(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT, REACTION MECHANISM. - Ref.12"Increasing the conformational entropy of the Omega-loop lid domain in phosphoenolpyruvate carboxykinase impairs catalysis and decreases catalytic fidelity."
Johnson T.A., Holyoak T.
Biochemistry 49:5176-5187(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATES, COFACTOR, SUBUNIT. - Ref.14"Three rare diseases in one sib pair: RAI1, PCK1, GRIN2B mutations associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA receptor glutamate insensitivity."
Adams D.R., Yuan H., Holyoak T., Arajs K.H., Hakimi P., Markello T.C., Wolfe L.A., Vilboux T., Burton B.K., Fajardo K.F., Grahame G., Holloman C., Sincan M., Smith A.C., Wells G.A., Huang Y., Vega H., Snyder J.P. , Golas G.A., Tifft C.J., Boerkoel C.F., Hanson R.W., Traynelis S.F., Kerr D.S., Gahl W.A.
Mol. Genet. Metab. 113:161-170(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MANGANESE; GTP AND SUBSTRATE, COFACTOR, SUBUNIT. - Ref.15"Inhibition and allosteric regulation of monomeric phosphoenolpyruvate carboxykinase by 3-mercaptopicolinic acid."
Balan M.D., Mcleod M.J., Lotosky W.R., Ghaly M., Holyoak T.
Biochemistry 54:5878-5887(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH 3-MERCAPTOPICOLINATE; GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION. - Ref.16"Utilization of substrate intrinsic binding energy for conformational change and catalytic function in phosphoenolpyruvate carboxykinase."
Johnson T.A., Mcleod M.J., Holyoak T.
Biochemistry 55:575-587(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH GTP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-89. - Ref.18"Characterization of 3-[(carboxymethyl)thio]picolinic acid: a novel inhibitor of phosphoenolpyruvate carboxykinase."
Mcleod M.J., Krismanich A.P., Assoud A., Dmitrienko G.I., Holyoak T.
Biochemistry 58:3918-3926(2019) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) IN COMPLEX WITH 3-[(CARBOXYMETHYL)THIO]PICOLINATE AND MANGANESE.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 263330, 1 interactor |
STRING: functional protein association networks More...STRINGi | 10116.ENSRNOP00000030913 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P07379 |
<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 | 5 – 9 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<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 | 12 – 14 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 15 – 18 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 20 – 22 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 25 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
Beta strandi | 40 – 45 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 50 – 62 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 65 – 69 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 72 – 74 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 76 – 78 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 84 – 86 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 89 – 91 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 92 – 95 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 99 – 102 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 107 – 109 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 119 – 127 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
<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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 131 – 134 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 137 – 148 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 155 – 162 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 164 – 173 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 174 – 177 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 178 – 184 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 190 – 195 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 214 – 216 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 218 – 222 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 223 – 225 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 227 – 232 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 236 – 239 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 242 – 248 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 249 – 258 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 261 – 264 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 266 – 271 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 277 – 283 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 286 – 289 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 290 – 294 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 304 – 311 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 313 – 317 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 323 – 326 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 330 – 335 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 341 – 343 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 345 – 350 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 356 – 359 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 361 – 363 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 388 – 391 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 395 – 397 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 405 – 409 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 410 – 412 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 418 – 421 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 426 – 434 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 438 – 440 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 443 – 446 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 450 – 458 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 461 – 463 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 466 – 469 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 475 – 477 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 479 – 481 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 483 – 485 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 490 – 499 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 500 – 502 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 510 – 514 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 521 – 523 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 525 – 527 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 530 – 533 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 534 – 544 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 550 – 553 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 556 – 559 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 561 – 563 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 567 – 569 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 574 – 578 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 582 – 599 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
Helixi | 601 – 603 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 606 – 620 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P07379 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P07379 |
<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
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 235 – 237 | Substrate binding5 Publications Manual assertion based on experiment ini
| 3 | |
Regioni | 403 – 405 | Substrate binding5 Publications Manual assertion based on experiment ini
| 3 | |
Regioni | 457 – 487 | Omega-loop1 Publication Manual assertion based on experiment ini
| 31 |
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3749, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00390000001912 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_028872_1_0_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P07379 |
Identification of Orthologs from Complete Genome Data More...OMAi | GPTNNWV |
Database of Orthologous Groups More...OrthoDBi | 286671at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P07379 |
TreeFam database of animal gene trees More...TreeFami | TF314402 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00819, PEPCK_GTP, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.449.10, 1 hit 3.90.228.20, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00452, PEPCK_GTP, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR018091, PEP_carboxykin_GTP_CS IPR013035, PEP_carboxykinase_C IPR008209, PEP_carboxykinase_GTP IPR035077, PEP_carboxykinase_GTP_C IPR035078, PEP_carboxykinase_GTP_N IPR008210, PEP_carboxykinase_N |
The PANTHER Classification System More...PANTHERi | PTHR11561, PTHR11561, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00821, PEPCK_GTP, 1 hit PF17297, PEPCK_N, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF001348, PEP_carboxykinase_GTP, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF68923, SSF68923, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00505, PEPCK_GTP, 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
MPPQLHNGLD FSAKVIQGSL DSLPQEVRKF VEGNAQLCQP EYIHICDGSE
60 70 80 90 100
EEYGRLLAHM QEEGVIRKLK KYDNCWLALT DPRDVARIES KTVIITQEQR
110 120 130 140 150
DTVPIPKSGQ SQLGRWMSEE DFEKAFNARF PGCMKGRTMY VIPFSMGPLG
160 170 180 190 200
SPLAKIGIEL TDSPYVVASM RIMTRMGTSV LEALGDGEFI KCLHSVGCPL
210 220 230 240 250
PLKKPLVNNW ACNPELTLIA HLPDRREIIS FGSGYGGNSL LGKKCFALRI
260 270 280 290 300
ASRLAKEEGW LAEHMLILGI TNPEGKKKYL AAAFPSACGK TNLAMMNPTL
310 320 330 340 350
PGWKVECVGD DIAWMKFDAQ GNLRAINPEN GFFGVAPGTS VKTNPNAIKT
360 370 380 390 400
IQKNTIFTNV AETSDGGVYW EGIDEPLAPG VTITSWKNKE WRPQDEEPCA
410 420 430 440 450
HPNSRFCTPA SQCPIIDPAW ESPEGVPIEG IIFGGRRPAG VPLVYEALSW
460 470 480 490 500
QHGVFVGAAM RSEATAAAEH KGKVIMHDPF AMRPFFGYNF GKYLAHWLSM
510 520 530 540 550
AHRPAAKLPK IFHVNWFRKD KNGKFLWPGF GENSRVLEWM FGRIEGEDSA
560 570 580 590 600
KLTPIGYVPK EDALNLKGLG DVNVEELFGI SKEFWEKEVE EIDKYLEDQV
610 620
NADLPYEIER ELRALKQRIS QM
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 | K03248 , K03243, K03244, K03245, K03246, K03247 Genomic DNA Translation: AAC98698.1 BC081900 mRNA Translation: AAH81900.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A23927, QYRTGP |
NCBI Reference Sequences More...RefSeqi | NP_942075.1, NM_198780.3 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENSRNOT00000031586; ENSRNOP00000030913; ENSRNOG00000028616 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 362282 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | rno:362282 |
<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 | |
---|---|---|---|---|---|---|
P07379 | Phosphoenolpyruvate carboxykinase, cytosolic [GTP] | 622 | UniRef90_P07379 | |||
Phosphoenolpyruvate carboxykinase (GTP) | 672 | |||||
Phosphoenolpyruvate carboxykinase (GTP) | 622 | |||||
Uncharacterized protein (Fragment) | 35 | |||||
Phosphoenolpyruvate carboxykinase (GTP) | 622 | |||||
+15 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P07379 | Phosphoenolpyruvate carboxykinase, cytosolic [GTP] | 622 | UniRef50_P07379 | |||
Phosphoenolpyruvate carboxykinase (GTP) | 672 | |||||
Phosphoenolpyruvate carboxykinase (GTP) | 622 | |||||
PEPCK_N domain-containing protein (Fragment) | 35 | |||||
Uncharacterized protein (Fragment) | 35 | |||||
+73 |
<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 | K03248 , K03243, K03244, K03245, K03246, K03247 Genomic DNA Translation: AAC98698.1 BC081900 mRNA Translation: AAH81900.1 |
PIRi | A23927, QYRTGP |
RefSeqi | NP_942075.1, NM_198780.3 |
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 |
2QEW | X-ray | 1.80 | A | 1-622 | [»] | |
2QEY | X-ray | 1.90 | A | 1-622 | [»] | |
2QF1 | X-ray | 1.80 | A | 1-622 | [»] | |
2QF2 | X-ray | 1.65 | A/B | 1-622 | [»] | |
2RK7 | X-ray | 1.90 | A/B | 1-622 | [»] | |
2RK8 | X-ray | 2.00 | A/B | 1-622 | [»] | |
2RKA | X-ray | 1.95 | A/C | 1-622 | [»] | |
2RKD | X-ray | 1.90 | A | 1-622 | [»] | |
2RKE | X-ray | 1.80 | A | 1-622 | [»] | |
3DT2 | X-ray | 1.50 | A | 1-622 | [»] | |
3DT4 | X-ray | 1.45 | A/C | 1-622 | [»] | |
3DT7 | X-ray | 1.50 | A/B | 1-622 | [»] | |
3DTB | X-ray | 1.30 | A/B | 1-622 | [»] | |
3MOE | X-ray | 1.25 | A | 1-622 | [»] | |
3MOF | X-ray | 1.75 | A/B | 1-622 | [»] | |
3MOH | X-ray | 2.10 | A/B | 1-622 | [»] | |
4GMM | X-ray | 1.74 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GMU | X-ray | 1.20 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GMW | X-ray | 1.75 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GMZ | X-ray | 2.05 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GNL | X-ray | 1.70 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GNM | X-ray | 1.50 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GNO | X-ray | 1.50 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GNP | X-ray | 1.74 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4GNQ | X-ray | 1.40 | A | 1-463 | [»] | |
A | 475-622 | [»] | ||||
4OX2 | X-ray | 2.00 | A/B | 1-622 | [»] | |
4YW8 | X-ray | 1.55 | A | 1-622 | [»] | |
4YW9 | X-ray | 1.40 | A | 1-622 | [»] | |
4YWB | X-ray | 1.50 | A/C | 1-622 | [»] | |
4YWD | X-ray | 2.10 | A | 1-622 | [»] | |
5FH0 | X-ray | 1.60 | A | 1-622 | [»] | |
5FH1 | X-ray | 1.55 | A | 1-622 | [»] | |
5FH2 | X-ray | 1.49 | A | 1-622 | [»] | |
5FH3 | X-ray | 1.60 | A | 1-622 | [»] | |
5FH4 | X-ray | 1.49 | A | 1-622 | [»] | |
5FH5 | X-ray | 1.55 | A | 1-622 | [»] | |
5V95 | X-ray | 2.30 | A | 1-622 | [»] | |
5V97 | X-ray | 1.80 | A | 1-622 | [»] | |
5V9F | X-ray | 2.05 | A | 1-622 | [»] | |
5V9G | X-ray | 1.95 | A | 1-622 | [»] | |
5V9H | X-ray | 2.15 | A/B | 1-622 | [»] | |
6P5O | X-ray | 1.49 | A | 1-622 | [»] | |
6YI9 | X-ray | 1.75 | A | 1-622 | [»] | |
SMRi | P07379 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 263330, 1 interactor |
STRINGi | 10116.ENSRNOP00000030913 |
Chemistry databases
BindingDBi | P07379 |
ChEMBLi | CHEMBL1075234 |
PTM databases
iPTMneti | P07379 |
PhosphoSitePlusi | P07379 |
Proteomic databases
jPOSTi | P07379 |
PaxDbi | P07379 |
PRIDEi | P07379 |
Genome annotation databases
Ensembli | ENSRNOT00000031586; ENSRNOP00000030913; ENSRNOG00000028616 |
GeneIDi | 362282 |
KEGGi | rno:362282 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5105 |
RGDi | 3267, Pck1 |
Phylogenomic databases
eggNOGi | KOG3749, Eukaryota |
GeneTreei | ENSGT00390000001912 |
HOGENOMi | CLU_028872_1_0_1 |
InParanoidi | P07379 |
OMAi | GPTNNWV |
OrthoDBi | 286671at2759 |
PhylomeDBi | P07379 |
TreeFami | TF314402 |
Enzyme and pathway databases
UniPathwayi | UPA00138 |
BRENDAi | 4.1.1.32, 5301 |
Reactomei | R-RNO-70263, Gluconeogenesis |
SABIO-RKi | P07379 |
Miscellaneous databases
EvolutionaryTracei | P07379 |
Protein Ontology More...PROi | PR:P07379 |
Gene expression databases
Bgeei | ENSRNOG00000028616, Expressed in kidney and 21 other tissues |
Genevisiblei | P07379, RN |
Family and domain databases
CDDi | cd00819, PEPCK_GTP, 1 hit |
Gene3Di | 3.40.449.10, 1 hit 3.90.228.20, 1 hit |
HAMAPi | MF_00452, PEPCK_GTP, 1 hit |
InterProi | View protein in InterPro IPR018091, PEP_carboxykin_GTP_CS IPR013035, PEP_carboxykinase_C IPR008209, PEP_carboxykinase_GTP IPR035077, PEP_carboxykinase_GTP_C IPR035078, PEP_carboxykinase_GTP_N IPR008210, PEP_carboxykinase_N |
PANTHERi | PTHR11561, PTHR11561, 1 hit |
Pfami | View protein in Pfam PF00821, PEPCK_GTP, 1 hit PF17297, PEPCK_N, 1 hit |
PIRSFi | PIRSF001348, PEP_carboxykinase_GTP, 1 hit |
SUPFAMi | SSF68923, SSF68923, 1 hit |
PROSITEi | View protein in PROSITE PS00505, PEPCK_GTP, 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 | PCKGC_RAT | |
<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 | P07379Primary (citable) accession number: P07379 | |
<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: | April 1, 1988 |
Last sequence update: | April 1, 1988 | |
Last modified: | April 7, 2021 | |
This is version 176 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 | Chordata 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, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families