true 2007-05-29 2008-06-10 13 ACEK_PSEAB Isocitrate dehydrogenase kinase/phosphatase EC 2.7.11.5 EC 3.1.3.- IDH kinase/phosphatase IDHK/P Lee D.G. Urbach J.M. Wu G. Liberati N.T. Feinbaum R.L. Miyata S. Diggins L.T. He J. Saucier M. Deziel E. Friedman L. Li L. Grills G. Montgomery K. Kucherlapati R. Rahme L.G. Ausubel F.M. doi:10.1186/gb-2006-7-10-r90 2006 Genome Biol. 7 RESEARCH90.1-RESEARCH90.14 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] aceK PA14_46450 Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation (By similarity). ATP + [isocitrate dehydrogenase (NADP(+))] = ADP + [isocitrate dehydrogenase (NADP(+))] phosphate. Cytoplasm (By similarity). Belongs to the aceK family. Isocitrate dehydrogenase kinase/phosphatase 1 577 ATP 318 324 374 374 ATP 339 339 EMBL RefSeq GeneID GenomeReviews PA14_46450 KEGG NMPDR HAMAP 1 InterPro IsoCit_DHase_AceK Pfam AceK 1 PIRSF AceK 1 HAMAP HAMAP HAMAP HAMAP HAMAP 2006-11-14 1 66761 MVQSAPASEI AALILRGFDD YREQFREITD GARARFEQAQ WQEAQRASTQ RINLYEEKVA ETVAGLRVGL ADSELLDVER WPIIKSAYIA QIDLRLDDEL AETWFNSIFC GLFSHDNISD GTMFVHTTRP SLRAHARAPY TRTYRPGGDL RQALEKIFDD YRFDVPYDDR ERDLERIDAL LHSNLPDWVC KDPDLAIELI GSVFYRNKGA YLVGRLFTPD EQWPLVFPLL HREGHGIQFD TVITDEAEVS IIFSFTRSYF MVDVPVPAEL VAFLKRLLPG KHLAELYTSI GFYKQGKSEF YRALINHLAT TDDRFVMAPG VRGMVMSVFT LPGFNTVFKI IKDRFNPSKS VDHATVIQKY QLVKNHDRVG RLADTQQFAD FRFPVSKFEP ECLAELLEVA PSTVVMEGDV VLIRHCWTER RMTPLNIYLE NASEAQTREA LNDYGLAIKQ LAAANIFPGD MLLKNFGVTR HGRVVFYDYD EICYLTEVNF RYIPEPRFPE DEMSSEPWYS VGPNDVFPEE FPRFLFVDLN QRRLFAKLHG NLYDAKYWQG LQEQIREGKV IDVFPYRRQE TPEQLLG