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Download torrent underwater game. You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser. aroK Escherichia coli (strain K12) Status Reviewed - Annotation score: - Experimental evidence at protein level i Function i Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. Miscellaneous Two isozymes have been found in AroK has 100-fold lower affinity for shikimate than AroL, suggesting that AroL is the dominant enzyme in the biosynthesis of the aromatic amino acids, with AroK playing a secondary role and possibly participating in an as yet unidentified cellular process. Catalytic activity i EC: 2. 7. 1. 71 Cofactor i Mg 2+ Note: Binds 1 Mg 2+ ion per subunit. Kinetics i K M = 20 mM for shikimate Pathway i: chorismate biosynthesis This protein is involved in step 5 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate. Proteins known to be involved in the 7 steps of the subpathway in this organism are: Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive ( aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase ( aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive ( aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive ( aroG) 3-dehydroquinate synthase ( aroB), 3-dehydroquinate synthase ( aroB), 3-dehydroquinate synthase ( aroB), 3-dehydroquinate synthase ( aroB), 3-dehydroquinate synthase ( aroB) 3-dehydroquinate dehydratase ( aroD), 3-dehydroquinate dehydratase ( aroD), 3-dehydroquinate dehydratase ( aroD), 3-dehydroquinate dehydratase ( aroD), 3-dehydroquinate dehydratase ( aroD) Quinate/shikimate dehydrogenase ( ydiB), Quinate/shikimate dehydrogenase ( ydiB), Quinate/shikimate dehydrogenase ( ydiB), Shikimate dehydrogenase (NADP(+)) ( aroE), Shikimate dehydrogenase (NADP(+)) ( aroE), Shikimate dehydrogenase (NADP(+)) ( aroE), Quinate/shikimate dehydrogenase ( ydiB), Shikimate dehydrogenase (NADP(+)) ( aroE), Quinate/shikimate dehydrogenase ( ydiB), Shikimate dehydrogenase (NADP(+)) ( aroE) Shikimate kinase 1 ( aroK), Shikimate kinase 2 ( aroL), Shikimate kinase 1 ( aroK), Shikimate kinase 2 ( aroL) 3-phosphoshikimate 1-carboxyvinyltransferase ( aroA), 3-phosphoshikimate 1-carboxyvinyltransferase ( aroA), 3-phosphoshikimate 1-carboxyvinyltransferase ( aroA), 3-phosphoshikimate 1-carboxyvinyltransferase ( aroA) Chorismate synthase ( aroC), Chorismate synthase ( aroC), Chorismate synthase ( aroC), Chorismate synthase ( aroC) This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis. View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis. Sites Feature key Position(s) Description Actions Graphical view Length Metal binding i 18 Magnesium 1 Binding site i 36 Substrate 1 Binding site i 60 Substrate 1 Binding site i 82 Substrate; via amide nitrogen 1 Binding site i 120 ATP 1 Binding site i 140 Substrate 1 Binding site i 157 ATP 1 Regions Feature key Position(s) Description Actions Graphical view Length Nucleotide binding i 14???19 ATP 6 GO - Molecular function i ATP binding magnesium ion binding shikimate kinase activity GO - Biological process i aromatic amino acid family biosynthetic process chorismate biosynthetic process response to antibiotic shikimate metabolic process Keywords i Enzyme and pathway databases Subcellular location i GO - Cellular component i cytosol Keywords - Cellular component i Cytoplasm PTM / Processing i Molecule processing Feature key Position(s) Description Actions Graphical view Length Initiator methionine i Removed Chain i PRO_0000192377 2???173 Shikimate kinase 1 Add BLAST 172 Proteomic databases 2D gel databases Expression i Induction i Constitutively expressed. Interaction i Subunit structure i Protein-protein interaction databases Structure i Secondary structure 1 173 Show more details 3D structure databases Miscellaneous databases Family & Domains i Region Feature key Position(s) Description Actions Graphical view Length Region i 116???127 Lid domain Add BLAST 12 Domain i The LID domain closes over the active site upon ATP binding. Sequence similarities i Phylogenomic databases Family and domain databases CDD i cd00464 SK?, 1 hit HAMAP i MF_00109 Shikimate_kinase?, 1 hit InterPro i View protein in InterPro IPR027417 P-loop_NTPase IPR031322 Shikimate/glucono_kinase IPR000623 Shikimate_kinase/TSH1 IPR023000 Shikimate_kinase_CS Pfam i View protein in Pfam PF01202 SKI?, 1 hit SUPFAM i SSF52540 SSF52540?, 1 hit PROSITE i View protein in PROSITE PS01128 SHIKIMATE_KINASE?, 1 hit Sequence i Sequence status i: Complete. Sequence processing i: The displayed sequence is further processed into a mature form. P0A6D7-1 [ UniParc] FASTA Add to basket ? Hide 10 20 30 40 50 MAEKRNIFLV GPMGAGKSTI GRQLAQQLNM EFYDSDQEIE KRTGADVGWV 60 70 80 90 100 FDLEGEEGFR DREEKVINEL TEKQGIVLAT GGGSVKSRET RNRLSARGVV 110 120 130 140 150 VYLETTIEKQ LARTQRDKKR PLLHVETPPR EVLEALANER NPLYEEIADV 160 170 TIRTDDQSAK VVANQIIHML ESN 173 19, 538 January 23, 2007 - v2 5681B562B5CD4674 GO Sequence caution i The sequence AAA58187 differs from that shown. Reason: Erroneous initiation. Extended N-terminus. The sequence AAC36834 differs from that shown. Reason: Frameshift. The sequence CAA79665 differs from that shown. Sequence databases Genome annotation databases Entry information i Entry name i AROK_ECOLI Accession i P0A6D7 Primary (citable) accession number: P0A6D7 Secondary accession number(s): P24167 Q8X4S0 Entry history i Integrated into UniProtKB/Swiss-Prot: June 7, 2005 Last sequence update: January 23, 2007 Last modified: December 11, 2019 This is version 123 of the entry and version 2 of the sequence. See complete history. Entry status i Reviewed (UniProtKB/Swiss-Prot) Annotation program Prokaryotic Protein Annotation Program.

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