HAMAP rule MF_00109
General rule information
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Accession | MF_00109 |
Dates | 1-JUN-2001 (Created) 19-NOV-2022 (Last updated, Version 44) |
Name | Shikimate_kinase |
Scope | Bacteria |
Templates | P0A6D7 (AROK_ECOLI); P9WPY3 (AROK_MYCTU): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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case not <OC:Enterobacterales>
Protein name |
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else case <OC:Enterobacterales>
Protein name |
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end case
Gene name |
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Comments
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Function | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. |
Catalytic activity | RHEA:13121: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
EC 2.7.1.71 |
Cofactor | Mg(2+) Note: Binds 1 Mg(2+) ion per subunit. |
Pathway | Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. |
Subunit | Monomer. |
Subcellular location | Cytoplasm. |
Similarity | Belongs to the shikimate kinase family. |
Keywords
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Cytoplasm
Amino-acid biosynthesis
Aromatic amino acid biosynthesis
ATP-binding
Kinase
Magnesium
Metal-binding
Nucleotide-binding
Transferase
Amino-acid biosynthesis
Aromatic amino acid biosynthesis
ATP-binding
Kinase
Magnesium
Metal-binding
Nucleotide-binding
Transferase
Gene Ontology
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GO:0000287; Molecular function: magnesium ion binding.
GO:0005524; Molecular function: ATP binding.
GO:0004765; Molecular function: shikimate kinase activity.
GO:0009073; Biological process: aromatic amino acid family biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
GO:0005524; Molecular function: ATP binding.
GO:0004765; Molecular function: shikimate kinase activity.
GO:0009073; Biological process: aromatic amino acid family biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
Cross-references
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Features
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From: AROK_MYCTU (P9WPY3) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 12 | 17 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | |||||||||
BINDING | 16 | 16 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420 | [ST] | ||||||||
BINDING | 34 | 34 | /ligand="substrate | D | ||||||||
BINDING | 58 | 58 | /ligand="substrate | R | ||||||||
BINDING | 80 | 80 | /ligand="substrate | G | ||||||||
BINDING | 117 | 117 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | [RK] | ||||||||
BINDING | 136 | 136 | /ligand="substrate | R | ||||||||
BINDING (Optional) | 153 | 153 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 | [RQ] |
Additional information
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Size range | 161-214 amino acids |
Related rules | MF_01269 (AROL supersedes the current rule); MF_03143 (ARO1 supersedes the current rule) |
Fusion | Nter: None; Cter: MF_00110 (aroB) |
Comments | Archaeal aroK belong to a separate family (MF_00370). Enterobacterales (except WIGBR, BLOBP, BLOFL, BUCAI, BUCAP and BUCBP) possess a second shikimate kinase (aroL, MF_01269). Mg(2+) is six-coordinated in shikimate kinase 1 (aroK, MF_00109) with direct interaction with two protein side-chains, whereas it is four-coordinated in shikimate kinase 2 (aroL, MF_01269) with direct interaction with only one protein side-chain. Strange longer C-terminus in FRACC; sequence not included in size range. |