HAMAP rule MF_01269
General rule information
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Accession | MF_01269 |
Dates | 18-MAY-2006 (Created)
19-NOV-2022 (Last updated, Version 21) |
Name | Shikimate_kinase_2 |
Scope(s) |
Bacteria Enterobacterales |
Template(s) | P10880 (AROL_DICCH); P0A6E1 (AROL_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_01269 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | AROL |
Protein name | RecName: Full=Shikimate kinase 2; Short=SK 2; EC=2.7.1.71; |
Gene name | Name=aroL; |
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. |
DOMAIN | The LID domain closes over the active site upon ATP binding. |
SIMILARITY | Belongs to the shikimate kinase family. AroL subfamily. |
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: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: AROL_DICCH (P10880) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 12 | 17 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-[CA]-G-K-T-T | ||||||||
REGION | 112 | 126 | /note="LID domain" | |||||||||
BINDING | 16 | 16 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
T | ||||||||
BINDING | 32 | 32 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | ||||||||
BINDING | 34 | 34 | /ligand="substrate" | D | ||||||||
BINDING | 58 | 58 | /ligand="substrate" | R | ||||||||
BINDING | 79 | 79 | /ligand="substrate" | G | ||||||||
BINDING | 120 | 120 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
BINDING | 139 | 139 | /ligand="substrate" | R | ||||||||
BINDING | 155 | 155 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
Q |
Additional information
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Size range | 173-181 amino acids |
Related rules |
MF_00109 |
Fusion | Nter: None Cter: None |
Comments | 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. |