AC   MF_00453;
DC   Protein; auto
TR   HAMAP; MF_00453; -; 1; level=0
XX
Names: PEPCK_ATP
XX
ID   PCKA
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP);
DE            Short=PEP carboxykinase;
DE            Short=PEPCK;
DE            EC=4.1.1.49;
DE            Short=PCK;
GN   Name=pckA;
XX
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC       oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC       phosphoryl transfer between the nucleoside triphosphate and OAA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=4.1.1.49;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 1 Mn(2+) ion per subunit.;
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
case <OC:Gammaproteobacteria>
CC   -!- SUBUNIT: Monomer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family.
XX
DR   Pfam; PF01293; PEPCK_ATP; 1; trigger=no
DR   NCBIfam; TIGR00224; PckA; 1; trigger=no
DR   PROSITE; PS00532; PEPCK_ATP; 1; trigger=no
XX
case <FT:15> or <FT:16>
KW   Acetylation
end case
KW   Cytoplasm
KW   Gluconeogenesis
KW   Lyase
KW   Decarboxylase
KW   ATP-binding
KW   Nucleotide-binding
KW   Metal-binding
KW   Manganese
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity
GO   GO:0006094; P:gluconeogenesis
GO   GO:0005737; C:cytoplasm
XX
FT   From: PCKA_ECOLI (P22259)
FT   BINDING         248..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-L-S-G-T-G-K-T-T
FT   BINDING         449..450
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [RK]-[IV]
FT   BINDING         213
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: K
FT   BINDING         232
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         269
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: D
FT   BINDING         65
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         207
FT                   /ligand="substrate"
FT   Condition: [YF]
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
FT   BINDING         213
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: H
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [ED]
FT   BINDING         333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         333
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         455
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [TS]
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         87
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         523
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
XX
Size: 493-542;
Related: None;
Template: P22259; A6VKV4; O09460; Q5SLL5;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in MOOTA, SALRD
Plasmid: 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.
XX
# Revision 1.33 2023/06/01
//