ID   ACEK_BURA4              Reviewed;         608 AA.
AC   B1YNR4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=BamMC406_2838;
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001025; ACB65314.1; -; Genomic_DNA.
DR   RefSeq; WP_012364824.1; NC_010551.1.
DR   AlphaFoldDB; B1YNR4; -.
DR   SMR; B1YNR4; -.
DR   EnsemblBacteria; ACB65314; ACB65314; BamMC406_2838.
DR   KEGG; bac:BamMC406_2838; -.
DR   HOGENOM; CLU_033804_1_1_4; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
DR   Proteomes; UP000001680; 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..608
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_1000133258"
FT   REGION          589..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         327..333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   608 AA;  70263 MW;  7F8DFCB8B2B43C3E CRC64;
     MNHFPKLLSS QIGFDVAQTM LENFDRHYRI FREAAVDAKT LYERADWHGL QRLARERITS
     YDDRVQECVE VLQDEYDAEN IDDEVWQQIK LHYIGLLTSH RQPECAETFF NSVCCKILHR
     SYFNNDFIFV RPAISTEYLE NDEPAAKPTY RAYYPGTDGL AATLERIVTN FQLEPPFEDL
     TRDIGCVMQA ITDEFGEFDA APNFQIHVLS SLFFRNKSAY IVGRIINADR VLPFAVPIRH
     VRPGLLALDT VLLRRDLLQI IFSFSHSYFL VDMGVPSAYV DFLCTIMPGK PKAEIYTSVG
     LQKQGKNLFY RDLLHHLSHS SDRFIIAPGI KGLVMLVFTL PSFPYVFKII KDHFPPPKET
     TREQIMEKYQ LVKRHDRLGR MADTLEYSSV ALPISRLDHA LVRELEKEVP SLLEYEDGNL
     VIKHLYIERR MIPLNLYLQN GTDAEIEHGV KEYGNAVKEL MKANIFPGDM LYKNFGVTRH
     GRVVFYDYDE IEYLTDCNVR RVPPPRNEED ELSGEPWYTV GPHDIFPETY GPFLLGDPRV
     RAVFMKHHAD FFEASLWQAS KDKLLQGELP DFYPYDVSLR FSVRYPDRFD STPDAGDGDS
     AGDAQRAA