Protein Domain : IPR008209

Type:  Family Name:  Phosphoenolpyruvate carboxykinase, GTP-utilising
Description:  Phosphoenolpyruvate carboxykinase (PEPCK) catalyses the first committed (rate-limiting) step in hepatic gluconeogenesis, namely the reversible decarboxylation of oxaloacetate to phosphoenolpyruvate (PEP) and carbon dioxide, using either ATP or GTP as a source of phosphate. The ATP-utilising () and GTP-utilising () enzymes form two divergent subfamilies, which have little sequence similarity but which retain conserved active site residues. ATP-utilising PEPCKs are monomers or oligomers of identical subunits found in certain bacteria, yeast, trypanosomatids, and plants, while GTP-utilising PEPCKs are mainly monomers found in animals and some bacteria []. Both require divalent cations for activity, such as magnesium or manganese. One cation interacts with the enzyme at metal binding site 1 to elicit activation, while the second cation interacts at metal binding site 2 to serve as a metal-nucleotide substrate. In bacteria, fungi and plants, PEPCK is involved in the glyoxylate bypass, an alternative to the tricarboxylic acid cycle.PEPCK helps to regulate blood glucose levels. The rate of gluconeogenesis can be controlled through transcriptional regulation of the PEPCK gene by cAMP (the mediator of glucagon and catecholamines), glucocorticoids and insulin. In general, PEPCK expression is induced by glucagon, catecholamines and glucocorticoids during periods of fasting and in response to stress, but is inhibited by (glucose-induced) insulin upon feeding []. With type II diabetes, this regulation system can fail, resulting in increased gluconeogenesis that in turn raises glucose levels [].PEPCK consists of an N-terminal and a catalytic C-terminal domain, with the active site and metal ions located in a cleft between them. Both domains have an alpha/beta topology that is partly similar to one another [, ]. Substrate binding causes PEPCK to undergo a conformational change, which accelerates catalysis by forcing bulk solvent molecules out of the active site []. PCK uses an alpha/beta/alpha motif for nucleotide binding, this motif differing from other kinase domains. GTP-utilising PEPCK has a PEP-binding domain and two kinase motifs to bind GTP and magnesium.This entry represents GTP-utilising phosphoenolpyruvate carboxykinase enzymes. Short Name:  PEP_carboxykinase_GTP
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0 Child Features

3 Contains

DB identifier Type Name
IPR008210 Domain Phosphoenolpyruvate carboxykinase, N-terminal
IPR013035 Domain Phosphoenolpyruvate carboxykinase, C-terminal
IPR018091 Conserved_site Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site

4 Cross Referencess

Identifier
PTHR11561
PF00821
PIRSF001348
MF_00452

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0004611 IPR008209
GO:0005525 IPR008209
GO:0006094 IPR008209

3 Ontology Annotations

GO Term Gene Name
GO:0004611 IPR008209
GO:0005525 IPR008209
GO:0006094 IPR008209

0 Parent Features

2 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Brdisv1pangenome1011682m.p PAC:33622467 Brachypodium distachyon Pangenome 614  
Brdisv1BdTR12c1041366m.p PAC:34404916 Brachypodium distachyon BdTR12c 614  

6 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8609605
            16330239
            15023367
            15890557
            16126724
            17403375