ID   ACEK_AERHH              Reviewed;         575 AA.
AC   A0KMM4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=AHA_3021;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39426.1; -; Genomic_DNA.
DR   RefSeq; WP_011706819.1; NC_008570.1.
DR   RefSeq; YP_857525.1; NC_008570.1.
DR   AlphaFoldDB; A0KMM4; -.
DR   SMR; A0KMM4; -.
DR   STRING; 380703.AHA_3021; -.
DR   EnsemblBacteria; ABK39426; ABK39426; AHA_3021.
DR   KEGG; aha:AHA_3021; -.
DR   PATRIC; fig|380703.7.peg.3023; -.
DR   eggNOG; COG4579; Bacteria.
DR   HOGENOM; CLU_033804_1_1_6; -.
DR   OMA; EPWYSVG; -.
DR   Proteomes; UP000000756; 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..575
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_0000288279"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         315..321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   575 AA;  67157 MW;  DFFCBAA9E00F527C CRC64;
     MQQPLEQAVA ETILQRFESF YSRFLEITQG SKSRFENSDW LGVQLAGRER IRLYDHHVGA
     TTALIKQMMG ATLPSQALLK QVKGAFSDLL PKCENFEVAE SFFNSVYRRI FRHRNIRDEN
     LYIHPFRSRG EHPDLSALLR IYRTDLAHLP QTLSQLLGDY SFTLPYEDKQ RDIVDIQRHL
     AENGPAILHD EPFAIELLKE VFYRNKGAYL VGLIRVKGQV FPFILPLLST GQSIYVDTVI
     FEPELASIVF GFARAYFMVY APMPALFVLF LRQIMPHKPD YEIYNAIGCQ KHGKTELYRH
     YQQHLAQSRE QFVIAPGIKG MVMSVFTLPS YDVVFKVIKD EFTPPKDVSH EQVKAKYRLV
     KQHDRVGRMA DTQEFTNFEF PLDRISPELL AELKTVAPSA LTLTDDKLVI KHLYTERKMI
     PLNLYLDKAD EQQTRLALEE YGNAIKQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC
     YMTECNFRQI PPPRYPEDEW SAEPWYSVAP NDIFPEEFAT FLLQKPQVRD IMMQLHKELF
     DANYWKMLQS NIKEGVFEDV YPYRRKKRFK FQRGG