HAMAP rule MF_00452
General rule information
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Accession | MF_00452 |
Dates | 23-SEP-2001 (Created) 19-NOV-2022 (Last updated, Version 38) |
Name | PEPCK_GTP |
Scope | Bacteria
Archaea |
Templates | Q9AEM1 (PCKG_CORGL); Q9AGJ6 (PCKG_MYCSM); Q6F494 (PCKG_THEKO); A5TYT6 (PCKG_MYCTA): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
Gene name |
|
Comments
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case <OS:Treponema pallidum>
Function | Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP). |
else
Function | Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. |
end case
Catalytic activity | RHEA:10388: GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate
EC 4.1.1.32 |
case <FTGroup:1>
Cofactor | Mn(2+) Note: Binds 1 Mn(2+) ion per subunit. |
end case
Pathway | Carbohydrate biosynthesis; gluconeogenesis. |
case <OC:Bacteria>
Subunit | Monomer. |
end case
Subcellular location | Cytoplasm. |
Similarity | Belongs to the phosphoenolpyruvate carboxykinase [GTP] family. |
Keywords
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case <FTGroup:1>
end case
Gene Ontology
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GO:0005525; Molecular function: GTP binding.
GO:0004613; Molecular function: phosphoenolpyruvate carboxykinase (GTP) activity.
GO:0004613; Molecular function: phosphoenolpyruvate carboxykinase (GTP) activity.
case <FTGroup:1>
GO:0030145; Molecular function: manganese ion binding.
end case
Cross-references
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Features
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From: PCKG_MYCTA (A5TYT6) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING (Optional) | 272 | 277 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565 | [AGSQM]-[CS]-G-K-T-[NS] | ||||||||
BINDING (Optional) | 515 | 518 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565 | [FY]-x-x-N | ||||||||
BINDING | 220 | 222 | /ligand="substrate | Y-x-G | ||||||||
BINDING | 387 | 389 | /ligand="substrate | N-x-R | ||||||||
ACT_SITE | 273 | 273 | [CS] | |||||||||
BINDING | 229 | 229 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035 | K | 1 | |||||||
BINDING | 249 | 249 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035 | H | 1 | |||||||
BINDING | 296 | 296 | /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035 | D | 1 | |||||||
BINDING | 81 | 81 | /ligand="substrate | R | ||||||||
BINDING | 271 | 271 | /ligand="substrate | S | ||||||||
BINDING | 389 | 389 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565 | R | ||||||||
BINDING | 420 | 420 | /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565 | R |
Additional information
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Size range | 588-624 amino acids |
Related rules | None |
Fusion | None |
Comments | The enzyme from THEKO is shown to be a homotetramer. |