AC   MF_00109;
DC   Protein; auto
TR   HAMAP; MF_00109; -; 1; level=0
XX
Names: Shikimate_kinase
XX
ID   AROK
case not <OC:Enterobacterales>
DE   RecName: Full=Shikimate kinase;
DE            Short=SK;
DE            EC=2.7.1.71;
else case <OC:Enterobacterales>
DE   RecName: Full=Shikimate kinase 1;
DE            Short=SK 1;
DE            EC=2.7.1.71;
end case
GN   Name=aroK;
XX
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl
CC       group of shikimic acid using ATP as a cosubstrate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
CC         Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
CC         EC=2.7.1.71;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       5/7.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the shikimate kinase family.
XX
DR   Pfam; PF01202; SKI; 1; trigger=no
DR   PRINTS; PR01100; SHIKIMTKNASE; 1; trigger=no
DR   PROSITE; PS01128; SHIKIMATE_KINASE; 1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   ATP-binding
KW   Kinase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Transferase
XX
GO   GO:0000287; F:magnesium ion binding
GO   GO:0005524; F:ATP binding
GO   GO:0004765; F:shikimate kinase activity
GO   GO:0009073; P:aromatic amino acid family biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: AROK_MYCTU (P9WPY3)
FT   BINDING         12..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [ST]
FT   BINDING         34
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         58
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         80
FT                   /ligand="substrate"
FT   Condition: G
FT   BINDING         117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [RK]
FT   BINDING         136
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [RQ]
XX
Size: 161-214;
Related: MF_01269!; MF_03143!;
Template: P0A6D7; P9WPY3;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: MF_00110 (aroB)
Duplicate: None
Plasmid: None
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.
XX
# Revision 1.44 2022/11/19
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