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HAMAP rule MF_00453

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General rule information [?]

Accession MF_00453
Dates 25-SEP-2001 (Created)
1-JUN-2023 (Last updated, Version 33)
Name PEPCK_ATP
Scope(s) Bacteria
Archaea
Template(s) P22259 (PCKA_ECOLI); A6VKV4 (PCKA_ACTSZ); O09460 (PCKA_ANASU); Q5SLL5 (PCKA_THET8); [ Recover all ]
Triggered by HAMAP; MF_00453 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PCKA
Protein name RecName: Full=Phosphoenolpyruvate carboxykinase (ATP);
                 Short=PEP carboxykinase;
                 Short=PEPCK;
                 EC=4.1.1.49;
                 Short=PCK;
Gene name Name=pckA;

Comments [?]

FUNCTIONInvolved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
CATALYTIC ACTIVITY Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate; Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=4.1.1.49;
COFACTOR Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 1 Mn(2+) ion per subunit.;
PATHWAYCarbohydrate biosynthesis; gluconeogenesis.
case <OC:Gammaproteobacteria>
SUBUNITMonomer.
end case
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the phosphoenolpyruvate carboxykinase (ATP) family.

Keywords [?]


Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0004612; Molecular function:phosphoenolpyruvate carboxykinase (ATP) activity
GO:0006094; Biological process:gluconeogenesis
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF01293; PEPCK_ATP; 1;
NCBIfam TIGR00224; PckA; 1;
PROSITE PS00532; PEPCK_ATP; 1;

Features [?]

From: PCKA_ECOLI (P22259)
Key From To Description Tag Condition FTGroup
BINDING 248 256 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
G-L-S-G-T-G-K-T-T
BINDING 449 450 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[RK]-[IV]
BINDING 213 213 /ligand="Mn(2+)"
/ligand_id="ChEBI:CHEBI:29035"
K
BINDING 232 232 /ligand="Mn(2+)"
/ligand_id="ChEBI:CHEBI:29035"
H
BINDING 269 269 /ligand="Mn(2+)"
/ligand_id="ChEBI:CHEBI:29035"
D
BINDING 65 65 /ligand="substrate" R
BINDING 207 207 /ligand="substrate" [YF]
BINDING 213 213 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
K
BINDING 213 213 /ligand="substrate" K
BINDING 232 232 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
H
BINDING 297 297 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[ED]
BINDING 333 333 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R
BINDING 333 333 /ligand="substrate" R
BINDING 455 455 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[TS]
case <OC:Escherichia> or <OC:Shigella>
MOD_RES 87 87 /note="N6-acetyllysine" K
MOD_RES 523 523 /note="N6-acetyllysine" K
end case

Additional information [?]

Size range 493-542 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments Probable C-terminally frameshifted DEIRA not taken into alignment and size range. Allosteric regulation by calcium ions is showed only in E.coli, S. typhimurium and T.thermophilus.



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