ID   ACEK_ACIAC              Reviewed;         602 AA.
AC   A1TVC1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Aave_4369;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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; CP000512; ABM34909.1; -; Genomic_DNA.
DR   RefSeq; WP_011797380.1; NC_008752.1.
DR   AlphaFoldDB; A1TVC1; -.
DR   SMR; A1TVC1; -.
DR   STRING; 397945.Aave_4369; -.
DR   EnsemblBacteria; ABM34909; ABM34909; Aave_4369.
DR   KEGG; aav:Aave_4369; -.
DR   eggNOG; COG4579; Bacteria.
DR   HOGENOM; CLU_033804_1_1_4; -.
DR   OrthoDB; 245269at2; -.
DR   Proteomes; UP000002596; Chromosome.
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; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..602
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_0000288277"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         325..331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   602 AA;  70101 MW;  745D93F92FD561D5 CRC64;
     MFPRRLDSPA AYGIAQAMMD GFDRHYRLFR AESARAKHRF ETSDWSGQQR AQRERIEFYD
     LRVKECVRRL EKEFSAGAQP MDVWHQVKLH YIGLLVGHRQ PELAETFFNS VTTKILHRTH
     FHNDFIFVRP AISTEYLEND EPGARPTYRA YYPTPESLQE TLVRVVDNFQ LQGEFEDLAR
     DAGRVAEVMR PRLGPAKWRA NFQIQVLSSL FYRNKGAYLV GKVINGFQEL AFALPILHGT
     DGRYVIDAAL FGEDDLQMLF SFARAYFMVD MEIPSAYVQF LRSLMPRKPR AELYNALGLA
     KQGKTLFYRD FLHHLRYSSD RFRIAPGIKG MVMLVFDLPS FPFVFKVIKD YYPPQKDTTR
     EQIKGKYLLV KQHDRVGRMA DTLEYSEVAF PRERFEDDLI AEIEKFAPSQ LEISDRDGDG
     NVEVILKHVY IERRMIPLNI YLQEAFDAGP HDARARQQME RSVVEYGNAI KDLVAANIFP
     GDMLWKNFGV TRNGKVVFYD YDEIEYLTDC HFRRVPAPRN EEDELSGEVW WAVGPRDVFP
     ETFGPFLLGN DAVREVFMRH HADLLDPVFW QSHKERIQAG HMYDVFPYDP ERRFGAGTGS
     PA