ID   ACEK_BURTA              Reviewed;         603 AA.
AC   Q2T1P5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=BTH_I0346;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC36516.1; -; Genomic_DNA.
DR   RefSeq; WP_009893275.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2T1P5; -.
DR   SMR; Q2T1P5; -.
DR   PRIDE; Q2T1P5; -.
DR   EnsemblBacteria; ABC36516; ABC36516; BTH_I0346.
DR   KEGG; bte:BTH_I0346; -.
DR   HOGENOM; CLU_033804_1_1_4; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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..603
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_0000259148"
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   603 AA;  70047 MW;  E6C0B30A99CEDF29 CRC64;
     MNHFPKLLSS QIGFDVAQTI LENFDRHYRI FREAAVEAKD LFERSDWHGL QRLARERITS
     YDDRVRECVE LLEDEYDAEN IDHDVWPQIK LHYIGLLTSH RQPECAETFF NSVCCKILHR
     AYFNNDFIFV RPAISTEYIE NDEPAAKPTY RAYYPGSEGL AATLERIVTN FQLNPPFEDL
     ERDIACIMQA IHDEFGAFDE AVNFQIHVLS SLFYRNKTAY IVGRIINGDR VLPFAVPIRH
     ARAGVLALDT VLLRRDQLKI IFSFSHSYFL VDMNVPSAYV QFLRSIMPGK PKAEIYTSVG
     LQKQGKNLFY RDLLHHLSHS SDRFIIAPGI KGLVMLVFTL PSFPYVFKMI KDHFPPPKET
     TREQIMDKYL LVKRHDRLGR MADTLEYSSV ALPLARLDDA LVRELEKEVP SLIEYEGDSL
     VIKHLYIERR MVPLNLYLQN GSDAEIEHGV REYGNAVKEL IQANIFPGDM LYKNFGVTRH
     GRVVFYDYDE IEYLTDCNVR RVPPPRNDED EMSGEPWYTV GPHDIFPETY APFLLGDPRV
     REHFLAHHAD FFDPQLWQDS KDRLLRGELP DFFAYEPALR FCLRYPERFA PGDAAEDGKR
     AAA