ID   ACEK_PSEMY              Reviewed;         572 AA.
AC   A4XT90;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Pmen_1792;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP84556.1; -; Genomic_DNA.
DR   RefSeq; WP_012018286.1; NC_009439.1.
DR   AlphaFoldDB; A4XT90; -.
DR   SMR; A4XT90; -.
DR   STRING; 399739.Pmen_1792; -.
DR   EnsemblBacteria; ABP84556; ABP84556; Pmen_1792.
DR   KEGG; pmy:Pmen_1792; -.
DR   PATRIC; fig|399739.8.peg.1818; -.
DR   eggNOG; COG4579; Bacteria.
DR   HOGENOM; CLU_033804_1_1_6; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
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..572
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_0000315269"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         317..323
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   572 AA;  66068 MW;  5CF79D7025A93DAE CRC64;
     MGQQWPAGEI ARLILDGFDD YREHFRQITD GARVRFEQAQ WQEAQRASAA RINLYEEKVA
     QTRERLLEGF DESLLEVGQW PLVKSAYIAL IDLRFDDELA ETWFNSIFCS LFSHDLISDG
     CMFIHTTRPS LRNQPSAAQT RNYRPAGELH LALQAIFDDY RFDVSYEDLP RDLQRLEGQL
     RASLPDWICK DPQQCIELFS SVLYRNKGAY LVGRIYTPDE QWPLVIPLLH REGLGIQVDA
     AITDEAEVSI IFSFTRSYFM VDVAIPAEFV GFLKRILPGK HIAELYTSIG FYKHGKSEFY
     RALIGHLAST DDRFIMAPGV RGMVMSVFTL PGFNTVFKII KDRFAHAKTV DRKTVIEKYR
     LVKSVDRVGR MADTQEFSDF RFPKAKFEPE CLAELLEVAP STVVVEGDTV LVRHCWTERR
     MTPLNLYLES ASEAQVREAL DDYGLAIKQL AAANIFPGDM LLKNFGVTRH GRVVFYDYDE
     ICFLTEVNFR RIPPPRFPED EMSSEPWYSV GPMDVFPEEF PPFLFADIKQ RRLFSQLHGN
     LYDADYWKQL QDAIRAGKVI DVFPYRRKSP VE