ID   ACEK_CUPTR              Reviewed;         615 AA.
AC   B2AG85;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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}; OrderedLocusNames=RALTA_A0111;
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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. {ECO:0000255|HAMAP-Rule:MF_00747}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H(+) + O-
CC         phospho-L-seryl-[isocitrate dehydrogenase]; 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00747}.
CC   -!- SIMILARITY: Belongs to the AceK family. {ECO:0000255|HAMAP-
CC       Rule:MF_00747}.
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DR   EMBL; CU633749; CAP62784.1; -; Genomic_DNA.
DR   RefSeq; WP_012351452.1; NC_010528.1.
DR   AlphaFoldDB; B2AG85; -.
DR   SMR; B2AG85; -.
DR   STRING; 977880.RALTA_A0111; -.
DR   EnsemblBacteria; CAP62784; CAP62784; RALTA_A0111.
DR   GeneID; 29762278; -.
DR   KEGG; cti:RALTA_A0111; -.
DR   eggNOG; COG4579; Bacteria.
DR   HOGENOM; CLU_033804_1_1_4; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
DR   BioCyc; CTAI977880:RALTA_RS00550-MON; -.
DR   Proteomes; UP000001692; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00747; AceK; 1.
DR   InterPro; IPR010452; Isocitrate_DH_AceK.
DR   PANTHER; PTHR39559; PTHR39559; 1.
DR   Pfam; PF06315; AceK; 1.
DR   PIRSF; PIRSF000719; AceK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glyoxylate bypass; Hydrolase; Kinase;
KW   Nucleotide-binding; Protein phosphatase; Serine/threonine-protein kinase;
KW   Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..615
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_1000133263"
FT   REGION          595..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        384
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         328..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         349
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   615 AA;  71671 MW;  9F7A057EBC4994F1 CRC64;
     MSHFPKLLSS QIAYDVARTM LDGFDKHYRL FREVSHQAKL KFEAGDWHGL QQIQRDRIAF
     YNERVRESSV ILEDEYDAEN IEDEIWQQIK LHYIGLLTNH HQPELAETFF NSVCTRILHR
     SYFNNDFIFV RPAISTEYIE NEESPTRPTF RAYYPGSREG MAACFERIVH NFQLERPFED
     LQRDIGYVVR AVGEHFGDLR IAPNFQIHTL SSLFFRNKAA FIIGRILNGD RTFPLAIPIL
     HGPSGKLVLD TVLLKKEQLL ILFSFTHSYF MVDMEIPSAY VTFLRDIMPR KPRAEIYTSL
     GLQKQGKNLF YRDFLHHLQH SSDKFIVAPG IRGLVMLVFT LPSYPYVFKV IRDVFPAPKE
     TTRELVKSKY QLVKQHDRVG RMADTLEYSD VAFPLSRFDE ALVREFEQHA PSMIEYQRAK
     DGGEEIVVRH VYIERRMTPL NIYLQEGSDA QVEHGVIEYG NAIKELIAAN IFPGDMLYKN
     FGVTRHGRVV FYDYDEIEYL TDCNIRHVPQ PRNEEEEMSG EVWYTVRPHD IFPETFRTFL
     LGDPRVGAAF LRHHADFFDP AMWQSHKDRL LAGHVHDFFA YHASDRFIHR YGAAAEPPAT
     PPVKQPDAGP ARRVA