HAMAP rule MF_00453
General rule information
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| 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
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Identifier, protein and gene names
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| 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
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| FUNCTION | Involved 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.; |
| PATHWAY | Carbohydrate biosynthesis; gluconeogenesis. |
| case <OC:Gammaproteobacteria> | |
| SUBUNIT | Monomer. |
| end case | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the phosphoenolpyruvate carboxykinase (ATP) family. |
Keywords
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| case <FT:15> or <FT:16> | |
| Acetylation | |
| end case | |
| Cytoplasm | |
| Gluconeogenesis | |
| Lyase | |
| Decarboxylase | |
| ATP-binding | |
| Nucleotide-binding | |
| Metal-binding | |
| Manganese | |
Gene Ontology
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| 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
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Features
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| 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
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| 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. |