HAMAP rule MF_00109
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00109 |
| Accession | MF_00109 |
| Dates | 28-FEB-2005 (Created)
02-SEP-2024 (Last updated, Version 37) |
| Name | Shikimate_kinase |
| Scope(s) |
Bacteria |
| Template(s) | P0A6D7; P9WPY3; [ 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=shikimate + ATP = 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. |