ID A0A6F8TUR3_9BACI Unreviewed; 169 AA. AC A0A6F8TUR3; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 14-DEC-2022, entry version 7. DE RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_00109}; DE Short=SK {ECO:0000256|HAMAP-Rule:MF_00109}; DE EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_00109}; GN Name=aroK {ECO:0000256|HAMAP-Rule:MF_00109, GN ECO:0000313|EMBL:BCB04714.1}; GN ORFNames=KH172YL63_28470 {ECO:0000313|EMBL:BCB04714.1}; OS Bacillus sp. KH172YL63. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=2709784 {ECO:0000313|EMBL:BCB04714.1, ECO:0000313|Proteomes:UP000500718}; RN [1] {ECO:0000313|EMBL:BCB04714.1, ECO:0000313|Proteomes:UP000500718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KH172YL63 {ECO:0000313|EMBL:BCB04714.1, RC ECO:0000313|Proteomes:UP000500718}; RA Murai Y., Masuda T., Onuma Y., Evans-Yamamoto D., Takeuchi N., Mori H., RA Masuyama N., Ishiguro S., Yachie D., Arakawa K.; RT "Complete Genome Sequence of Bacillus sp. Strain KH172YL63, Isolated from RT Deep-Sea Sediment."; RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000256|HAMAP- CC Rule:MF_00109}. 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; Evidence={ECO:0000256|HAMAP-Rule:MF_00109}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00109}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00109}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step CC 5/7. {ECO:0000256|HAMAP-Rule:MF_00109}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00109}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}. CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000256|HAMAP- CC Rule:MF_00109}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP022842; BCB04714.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6F8TUR3; -. DR UniPathway; UPA00053; UER00088. DR Proteomes; UP000500718; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd00464; SK; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00109; Shikimate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR031322; Shikimate/glucono_kinase. DR InterPro; IPR000623; Shikimate_kinase/TSH1. DR Pfam; PF01202; SKI; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00109}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141, KW ECO:0000256|HAMAP-Rule:MF_00109}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00109}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00109}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00109, ECO:0000313|EMBL:BCB04714.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00109}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00109}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00109}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00109}. FT BINDING 11..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 15 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 33 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 57 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" FT BINDING 151 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00109" SQ SEQUENCE 169 AA; 19286 MW; 250CE697F0561DC8 CRC64; MEPLYFIGFM GVGKTTIGKR LGEVLNLPVV DMDSYIEENE GTTIKEIFNH HGESYFRDLE SEALMKLSGT PAIITTGGGV VEREENRQLL RGKHQVFHLT CPFDVLWSRL EGDENRPLVQ KNSKERLSSL YNRRLPLYES CNGFDIETKD QTVEEVVQSI LHNLKGRAE //