ID   ACEK_ALBFT              Reviewed;         615 AA.
AC   Q21RR4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, 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=Rfer_3840;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-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; CP000267; ABD71539.1; -; Genomic_DNA.
DR   RefSeq; WP_011466102.1; NC_007908.1.
DR   AlphaFoldDB; Q21RR4; -.
DR   SMR; Q21RR4; -.
DR   STRING; 338969.Rfer_3840; -.
DR   EnsemblBacteria; ABD71539; ABD71539; Rfer_3840.
DR   KEGG; rfr:Rfer_3840; -.
DR   eggNOG; COG4579; Bacteria.
DR   HOGENOM; CLU_033804_1_1_4; -.
DR   OMA; EPWYSVG; -.
DR   OrthoDB; 245269at2; -.
DR   Proteomes; UP000008332; 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..615
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_0000288297"
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   615 AA;  71666 MW;  716ED446F0A86DEC CRC64;
     MFPTRLDSSL AYDIAKAMMD GFNRHYRLFR TESARAKHRF ETADWHGQQR AQRDRIEFYD
     LRVRECFMRL AREFKADEQP MEVWQQVKLH YIGLLVDHHQ PELAETFFNS VTTKILHHSY
     FQNDFIFVRP AVSTEYIEND ESETSPTYRS YYPTHDSLAE VLVQMVLDFD LRCPFADLDS
     DAARVQAAMV EQLGEVKLRA NFQLQVLSGL FFRNKGCYIV GKLINGFNEF PFALPVLYGR
     AGQLVIDAVL FGEDDLLMLF SFARAYFMVD MEIPSAYVQY LRSMMPRKPR NEIYNALGLA
     KQGKTLFYRD FLHHQRHSTD KFRIAPGIKG MVMLVFDLPS FPYVFKVIKD FYPPPKDTTR
     EQIKAKYLLV KQHDRVGRMA DTLEYSEVGF PRARFDDELI AELEKFAPSQ LEISDRDGDG
     RIEVIIKHVY IERRMIPLNI YLQEAFDAGG ANPDDTSPAA LRAREQIERG VIEYGNALKD
     LVAANIFPGD MLWKNFGITR HGKVVFYDYD EIEYITDCNF RKVPQARNEE DEMSGEVWYR
     VGPKDVFPET FAPFLLGNPF VREVFMKHHA ELLDAAFWQS HKERIQAGHV YDVFPYDQGK
     RFHPEISDAQ VPSSI