ID AROK_HAEIN Reviewed; 180 AA. AC P43880; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 04-NOV-2026, entry version 146. 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=HI_0207; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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=shikimate + ATP = 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; L42023; AAC21875.1; -; Genomic_DNA. DR PIR; F64054; F64054. DR AlphaFoldDB; P43880; -. DR SMR; P43880; -. DR STRING; 71421.HI_0207; -. DR EnsemblBacteria; AAC21875; AAC21875; HI_0207. DR KEGG; hin:HI_0207; -. DR PATRIC; fig|71421.8.peg.212; -. DR eggNOG; COG0703; Bacteria. DR HOGENOM; CLU_057607_2_2_6; -. DR OMA; AADIVKW; -. DR OrthoDB; 9800332at2; -. DR PhylomeDB; P43880; -. DR BioCyc; HINF71421:G1GJ1-218-MONOMER; -. DR UniPathway; UPA00053; UER00088. DR Proteomes; UP000000579; 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:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00464; SK; 1. DR FunFam; 3.40.50.300:FF:000099; Shikimate kinase 1; 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 NCBIfam; NF003456; aroK; 1. DR PANTHER; PTHR21087; SHIKIMATE KINASE; 1. DR PANTHER; PTHR21087:SF16; SHIKIMATE KINASE 1, CHLOROPLASTIC; 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 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding; KW Cytoplasm; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1..180 FT /note="Shikimate kinase" FT /id="PRO_0000192385" FT BINDING 14..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 18 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 36 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 60 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 82 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 120 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" FT BINDING 157 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00109" SQ SEQUENCE 180 AA; 20292 MW; E430C65F542B0C84 CRC64; MAEKRNIFLV GPMGAGKSTI GRQLAQQLNM DFIDSDAVIE ERTGADISWI FDLEGEDGFR KREERIINEL TQMQGIVLST GGGAVLSKEN RNYLSARGIV IYLETTVEKQ FQRTQRDKKR PLLQDAENPR QVLEDLAKIR NPLYEEIADI TLPTDEQNAK IMVNQIVDLI DNMNGLNGAL //