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HAMAP rule MF_00109
General rule information
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Accession | MF_00109 |
Dates | 1-JUN-2001 (Created)
12-MAR-2024 (Last updated, Version 45) |
Name | Shikimate_kinase |
Scope(s) |
Bacteria |
Template(s) | P0A6D7 (AROK_ECOLI); P9WPY3 (AROK_MYCTU); [ Recover all ] |
Triggered by |
HAMAP; MF_00109 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | AROK |
case not <OC:Enterobacterales> | |
Protein name | RecName: Full=Shikimate kinase; Short=SK; EC=2.7.1.71; |
else case <OC:Enterobacterales> | |
Protein name | RecName: Full=Shikimate kinase 1; Short=SK 1; EC=2.7.1.71; |
end case | |
Gene name | Name=aroK; |
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 | Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; 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 |
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:0009423; Biological process:chorismate 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 | 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 MF_03143 |
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. |