ID   ACEK_PSEPW              Reviewed;         569 AA.
AC   B1JCS1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=PputW619_3866;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000949; ACA74347.1; -; Genomic_DNA.
DR   RefSeq; WP_012315690.1; NC_010501.1.
DR   AlphaFoldDB; B1JCS1; -.
DR   SMR; B1JCS1; -.
DR   STRING; 390235.PputW619_3866; -.
DR   EnsemblBacteria; ACA74347; ACA74347; PputW619_3866.
DR   KEGG; ppw:PputW619_3866; -.
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..569
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_1000133274"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         316..322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         337
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   569 AA;  65929 MW;  EB2535206592D53A CRC64;
     MTQHWPAGEI ARMILDGFDD YREHFRRITL GARERFEQAR WQDIQRAAAA RINLYEQKVG
     EVNGWLRDGF DEEVLLEVEQ WPLVKSAYIR LIDPRLDDEL AETWYNSLFC SLFSHDQISD
     GCMFIHTTRP SIRSHERAAQ TRTYMPDGSL KGLVRAIFRD YAFDYGDLES DLSRLEEQLR
     DCLPDWVCKD PALAVELFVP VLYRNKGAYL VGRLYNSDEQ WPLVIPLLHR EGHGIEADAL
     ITDEAEVSII FSFTRSYFMV DVPVPAEFVN FLKRILPGKH IAELYTSIGF YKHGKSEFYR
     ALINHLASTD DRFIMAPGVR GMVMSVFTLP GFNTVFKIIK DRFSPSKTVD RATVIDKYRL
     VKSVDRVGRM ADTQEFADFR FPRGKFEPEC LAELLEVAPS TVAVEGDTVL VRHCWTERRM
     IPLNLYLEQA SEGQVLEALE DYGLAIKQLA AANIFPGDML LKNFGVTRHG RVVFYDYDEI
     SYLTEVNFRH IPPPRYPEDE MSGEPWYSIG PHDVFPEEFP PFLFADMGQR RLFSRLHGEL
     YDADYWKGLQ ASIREGKVID VFPYRRKGR