ID ACEK_ECOLI Reviewed; 578 AA. AC P11071; P11070; Q2M6T8; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 04-NOV-2026, entry version 191. DE RecName: Full=Isocitrate dehydrogenase kinase/phosphatase {ECO:0000255|HAMAP-Rule:MF_00747}; DE Short=IDH kinase/phosphatase {ECO:0000255|HAMAP-Rule:MF_00747}; DE Short=IDHK/P {ECO:0000255|HAMAP-Rule:MF_00747}; DE EC=2.7.11.5 {ECO:0000255|HAMAP-Rule:MF_00747}; DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_00747}; GN Name=aceK {ECO:0000255|HAMAP-Rule:MF_00747}; GN OrderedLocusNames=b4016, JW3976; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2836370; DOI=10.1128/jb.170.6.2763-2769.1988; RA Klumpp D.J., Plank D.W., Bowdin L.J., Stueland C.S., Chung T., RA Laporte D.C.; RT "Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase RT kinase/phosphatase."; RL J. Bacteriol. 170:2763-2769(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2826408; DOI=10.1128/jb.170.1.89-97.1988; RA Cortay J.-C., Bleicher F., Rieul C., Reeves H.C., Cozzone A.J.; RT "Nucleotide sequence and expression of the aceK gene coding for isocitrate RT dehydrogenase kinase/phosphatase in Escherichia coli."; RL J. Bacteriol. 170:89-97(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region RT from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55. RX PubMed=3049537; DOI=10.1128/jb.170.10.4528-4536.1988; RA Matsuoka M., McFadden B.A.; RT "Isolation, hyperexpression, and sequencing of the aceA gene encoding RT isocitrate lyase in Escherichia coli."; RL J. Bacteriol. 170:4528-4536(1988). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 552-578. RX PubMed=1995429; DOI=10.1016/0378-1119(91)90024-6; RA Galinier A., Bleicher F., Negre D., Perriere G., Duclos B., Cozzone A.J., RA Cortay J.-C.; RT "Primary structure of the intergenic region between aceK and iclR in the RT Escherichia coli chromosome."; RL Gene 97:149-150(1991). RN [8] RP REVIEW, AND MUTAGENESIS OF LYS-336. RX PubMed=2557093; DOI=10.1016/0300-9084(89)90110-7; RA Laporte D.C., Stueland C.S., Ikeda T.P.; RT "Isocitrate dehydrogenase kinase/phosphatase."; RL Biochimie 71:1051-1057(1989). RN [9] RP MUTAGENESIS OF ASP-371; ASN-377; ASP-403 AND GLU-439. RX PubMed=11258918; DOI=10.1021/bi001713x; RA Oudot C., Cortay J.-C., Blanchet C., Laporte D.C., Di Pietro A., RA Cozzone A.J., Jault J.-M.; RT "The 'catalytic' triad of isocitrate dehydrogenase kinase/phosphatase from RT E. coli and its relationship with that found in eukaryotic protein RT kinases."; RL Biochemistry 40:3047-3055(2001). CC -!- FUNCTION: Bifunctional enzyme which can phosphorylate or CC dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine CC residue. This is a regulatory mechanism which enables bacteria to CC bypass the Krebs cycle via the glyoxylate shunt in response to the CC source of carbon. When bacteria are grown on glucose, IDH is fully CC active and unphosphorylated, but when grown on acetate or ethanol, the CC activity of IDH declines drastically concomitant with its CC phosphorylation. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[isocitrate dehydrogenase] + ATP = O-phospho-L-seryl- CC [isocitrate dehydrogenase] + ADP + H(+); Xref=Rhea:RHEA:43540, CC Rhea:RHEA-COMP:10605, Rhea:RHEA-COMP:10606, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, CC ChEBI:CHEBI:456216; EC=2.7.11.5; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00747}; CC -!- INTERACTION: CC P11071; P08200: icd; NbExp=5; IntAct=EBI-1112800, EBI-369069; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the AceK family. {ECO:0000255|HAMAP- CC Rule:MF_00747}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA24007.1; Type=Frameshift; Evidence={ECO:0000305}; 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; M20714; AAA24010.1; -; Genomic_DNA. DR EMBL; M18974; AAA24007.1; ALT_FRAME; Genomic_DNA. DR EMBL; U00006; AAC43110.1; -; Genomic_DNA. DR EMBL; U00096; AAC76986.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78018.1; -; Genomic_DNA. DR EMBL; M22621; AAC13651.1; -; Genomic_DNA. DR EMBL; M63497; AAA73005.1; -; Genomic_DNA. DR PIR; G65208; KIECID. DR RefSeq; NP_418440.1; NC_000913.3. DR RefSeq; WP_001137220.1; NZ_CP009789.1. DR PDB; 6K5L; X-ray; 2.55 A; A/B=1-578. DR AlphaFoldDB; P11071; -. DR SMR; P11071; -. DR BioGRID; 4261467; 16. DR BioGRID; 849198; 7. DR DIP; DIP-9041N; -. DR FunCoup; P11071; 40. DR IntAct; P11071; 12. DR STRING; 511145.b4016; -. DR jPOST; P11071; -. DR PaxDb; 511145-b4016; -. DR DNASU; 944797; -. DR EnsemblBacteria; AAC76986; AAC76986; b4016. DR GeneID; 944797; -. DR KEGG; ecj:JW3976; -. DR KEGG; eco:b4016; -. DR KEGG; ecoc:C3026_21695; -. DR PATRIC; fig|1411691.4.peg.2697; -. DR EchoBASE; EB0025; -. DR eggNOG; COG4579; Bacteria. DR HOGENOM; CLU_033804_1_1_6; -. DR InParanoid; P11071; -. DR OMA; AADWHGQ; -. DR OrthoDB; 5287793at2; -. DR PhylomeDB; P11071; -. DR BioCyc; EcoCyc:ICITDEHASE-KIN-PHOSPHA; -. DR BioCyc; MetaCyc:ICITDEHASE-KIN-PHOSPHA; -. DR BRENDA; 2.7.11.5; 2026. DR SABIO-RK; P11071; -. DR PRO; PR:P11071; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P11071; -. DR GO; GO:0005737; C:cytoplasm; IC:EcoliWiki. DR GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IDA:EcoCyc. DR GO; GO:0016208; F:AMP binding; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki. DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc. DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:EcoCyc. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:EcoCyc. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006097; P:glyoxylate cycle; IC:EcoliWiki. DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:EcoCyc. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:EcoCyc. DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:EcoliWiki. DR HAMAP; MF_00747; AceK; 1. DR InterPro; IPR046855; AceK_kinase. DR InterPro; IPR046854; AceK_regulatory. DR InterPro; IPR010452; Isocitrate_DH_AceK. DR NCBIfam; NF002804; aceK; 1. DR PANTHER; PTHR39559; -; 1. DR PANTHER; PTHR39559:SF1; ISOCITRATE DEHYDROGENASE KINASE_PHOSPHATASE; 1. DR Pfam; PF06315; AceK_kinase; 1. DR Pfam; PF20423; AceK_regulatory; 1. DR PIRSF; PIRSF000719; AceK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; KW Glyoxylate bypass; Hydrolase; Kinase; Nucleotide-binding; KW Protein phosphatase; Reference proteome; Serine/threonine-protein kinase; KW Transferase; Tricarboxylic acid cycle. FT CHAIN 1..578 FT /note="Isocitrate dehydrogenase kinase/phosphatase" FT /id="PRO_0000057898" FT ACT_SITE 371 FT /evidence="ECO:0000305" FT BINDING 315..321 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747" FT BINDING 336 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747" FT MUTAGEN 336 FT /note="K->M: Inhibits enzyme." FT /evidence="ECO:0000269|PubMed:2557093" FT MUTAGEN 371 FT /note="D->A,E,Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:11258918" FT MUTAGEN 377 FT /note="N->A: No loss of activity." FT /evidence="ECO:0000269|PubMed:11258918" FT MUTAGEN 403 FT /note="D->A: No loss of activity." FT /evidence="ECO:0000269|PubMed:11258918" FT MUTAGEN 439 FT /note="E->A: No loss of activity." FT /evidence="ECO:0000269|PubMed:11258918" FT CONFLICT 140 FT /note="A -> G (in Ref. 2; AAA24007)" FT /evidence="ECO:0000305" FT CONFLICT 416..417 FT /note="ER -> DG (in Ref. 1; AAA24010)" FT /evidence="ECO:0000305" FT HELIX 2..29 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 31..36 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 40..69 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 76..88 FT /evidence="ECO:0007829|PDB:6K5L" FT TURN 89..92 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 96..110 FT /evidence="ECO:0007829|PDB:6K5L" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:6K5L" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:6K5L" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 150..159 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 169..184 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 186..191 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 206..215 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 218..228 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 243..249 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 264..272 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 280..286 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 290..307 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 321..327 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 332..338 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 350..361 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 372..381 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 387..396 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 401..404 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 407..417 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 422..425 FT /evidence="ECO:0007829|PDB:6K5L" FT TURN 426..428 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 431..450 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 460..462 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 463..465 FT /evidence="ECO:0007829|PDB:6K5L" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 482..484 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 515..517 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 518..522 FT /evidence="ECO:0007829|PDB:6K5L" FT TURN 526..528 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 529..536 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 537..540 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 542..553 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 565..567 FT /evidence="ECO:0007829|PDB:6K5L" FT HELIX 569..572 FT /evidence="ECO:0007829|PDB:6K5L" SQ SEQUENCE 578 AA; 67699 MW; 5ABD5FB5FA1D9B29 CRC64; MPRGLELLIA QTILQGFDAQ YGRFLEVTSG AQQRFEQADW HAVQQAMKNR IHLYDHHVGL VVEQLRCITN GQSTDAAFLL RVKEHYTRLL PDYPRFEIAE SFFNSVYCRL FDHRSLTPER LFIFSSQPER RFRTIPRPLA KDFHPDHGWE SLLMRVISDL PLRLRWQNKS RDIHYIIRHL TETLGTDNLA ESHLQVANEL FYRNKAAWLV GKLITPSGTL PFLLPIHQTD DGELFIDTCL TTTAEASIVF GFARSYFMVY APLPAALVEW LREILPGKTT AELYMAIGCQ KHAKTESYRE YLVYLQGCNE QFIEAPGIRG MVMLVFTLPG FDRVFKVIKD RFAPQKEMSA AHVRACYQLV KEHDRVGRMA DTQEFENFVL EKRHISPALM ELLLQEAAEK ITDLGEQIVI RHLYIERRMV PLNIWLEQVE GQQLRDAIEE YGNAIRQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC YMTEVNFRDI PPPRYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF RADYWRALQN RIREGHVEDV YAYRRRQRFS VRYGEMLF //