ID AROK_COXBU Reviewed; 179 AA. AC Q83AJ3; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Shikimate kinase {ECO:0000255|HAMAP-Rule:MF_00109}; DE Short=SK {ECO:0000255|HAMAP-Rule:MF_00109}; DE EC=2.7.1.71 {ECO:0000255|HAMAP-Rule:MF_00109}; GN Name=aroK {ECO:0000255|HAMAP-Rule:MF_00109}; GN OrderedLocusNames=CBU_1892; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae; OC Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). CC -!- FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl CC group of shikimic acid using ATP as a cosubstrate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00109}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00109}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00109}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00109}. CC -!- SIMILARITY: Belongs to the shikimate kinase family. {ECO:0000255|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; AE016828; AAO91383.1; -; Genomic_DNA. DR RefSeq; NP_820869.1; NC_002971.3. DR RefSeq; WP_010958519.1; NZ_CCYB01000008.1. DR PDB; 3TRF; X-ray; 2.60 A; A/B=1-179. DR PDBsum; 3TRF; -. DR AlphaFoldDB; Q83AJ3; -. DR SMR; Q83AJ3; -. DR STRING; 227377.CBU_1892; -. DR EnsemblBacteria; AAO91383; AAO91383; CBU_1892. DR GeneID; 1209805; -. DR KEGG; cbu:CBU_1892; -. DR PATRIC; fig|227377.7.peg.1875; -. DR eggNOG; COG0703; Bacteria. DR HOGENOM; CLU_057607_2_2_6; -. DR OrthoDB; 9800332at2; -. DR UniPathway; UPA00053; UER00088. DR EvolutionaryTrace; Q83AJ3; -. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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; IBA:GO_Central. 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; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR023000; Shikimate_kinase_CS. DR PANTHER; PTHR21087; SHIKIMATE KINASE; 1. DR PANTHER; PTHR21087:SF16; SHIKIMATE KINASE 1, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF01202; SKI; 1. DR PRINTS; PR01100; SHIKIMTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS01128; SHIKIMATE_KINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..179 FT /note="Shikimate kinase" FT /id="PRO_0000237869" FT BINDING 15..20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 19 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 37 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 123 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 18..29 FT /evidence="ECO:0007829|PDB:3TRF" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 36..44 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 48..73 FT /evidence="ECO:0007829|PDB:3TRF" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:3TRF" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 89..98 FT /evidence="ECO:0007829|PDB:3TRF" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 108..116 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 129..149 FT /evidence="ECO:0007829|PDB:3TRF" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:3TRF" FT HELIX 161..171 FT /evidence="ECO:0007829|PDB:3TRF" SQ SEQUENCE 179 AA; 20335 MW; A47C31B7EF35941C CRC64; MKKNLTNIYL IGLMGAGKTS VGSQLAKLTK RILYDSDKEI EKRTGADIAW IFEMEGEAGF RRREREMIEA LCKLDNIILA TGGGVVLDEK NRQQISETGV VIYLTASIDT QLKRIGQKGE MRRPLFIKNN SKEKLQQLNE IRKPLYQAMA DLVYPTDDLN PRQLATQILV DIKQTYSDL //