AC MF_00452; DC Protein; auto TR HAMAP; MF_00452; -; 1; level=0 XX Names: PEPCK_GTP XX ID PCKG DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP]; DE Short=PEP carboxykinase; DE Short=PEPCK; DE EC=4.1.1.32; DE AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase; DE Short=GTP-PEPCK; GN Name=pckG; XX case CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to CC phosphoenolpyruvate (PEP). else CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic CC pathway that produces glucose from lactate and other precursors derived CC from the citric acid cycle. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; case CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 Mn(2+) ion per subunit.; end case CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. case CC -!- SUBUNIT: Monomer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP] CC family. XX DR Pfam; PF00821; PEPCK; 1; trigger=no DR PROSITE; PS00505; PEPCK_GTP; 1; trigger=no XX KW Cytoplasm KW Decarboxylase KW Gluconeogenesis KW GTP-binding KW Lyase case KW Manganese KW Metal-binding end case KW Nucleotide-binding XX GO GO:0005525; F:GTP binding GO GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity case GO GO:0030145; F:manganese ion binding end case GO GO:0006094; P:gluconeogenesis GO GO:0005737; C:cytoplasm XX FT From: PCKG_MYCTA (A5TYT6) FT BINDING 272..277 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Optional; Condition: [AGSQM]-[CS]-G-K-T-[NS] FT BINDING 515..518 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Optional; Condition: [FY]-x-x-N FT BINDING 220..222 FT /ligand="substrate" FT Condition: Y-x-G FT BINDING 387..389 FT /ligand="substrate" FT Condition: N-x-R FT ACT_SITE 273 FT Condition: [CS] FT BINDING 229 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: K FT BINDING 249 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: H FT BINDING 296 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: D FT BINDING 81 FT /ligand="substrate" FT Condition: R FT BINDING 271 FT /ligand="substrate" FT Condition: S FT BINDING 389 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R FT BINDING 420 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: R XX Size: 588-624; Related: None; Template: Q9AEM1; Q9AGJ6; Q6F494; A5TYT6; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: The enzyme from THEKO is shown to be a homotetramer. XX # Revision 1.38 2022/11/19 //