ID   ACEK_PSEU5              Reviewed;         573 AA.
AC   A4VMC4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
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=PST_2473;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABP80125.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000304; ABP80125.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_013983082.1; NC_009434.1.
DR   AlphaFoldDB; A4VMC4; -.
DR   SMR; A4VMC4; -.
DR   STRING; 379731.PST_2473; -.
DR   EnsemblBacteria; ABP80125; ABP80125; PST_2473.
DR   KEGG; psa:PST_2473; -.
DR   eggNOG; COG4579; Bacteria.
DR   HOGENOM; CLU_033804_1_1_6; -.
DR   Proteomes; UP000000233; 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..573
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_0000315271"
FT   ACT_SITE        374
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         318..324
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ   SEQUENCE   573 AA;  66310 MW;  C03135DC9CC7FB71 CRC64;
     MVQHELAAEI ARQILLGFDD YREHFRLITE GARARFEQAQ WQEAQRASAA RISLYEEKVG
     ETRRRLLASF DHADLLQVEA WPQIKSAYIE LINPRFDDEL SETWYNSIFC GLFSHDCISD
     GTMFIHTTRP AVRAHERLAQ TRRYRPNGDL RGMLEQILRD YAFSVPYCDL PGDLQRLQTQ
     LCETLPDWVC KDPELTVEVF VSVLYRNKGA YLIGRIFTCD EQWPLAIPLL HRDGQGIVAD
     ALITDEAEVS IIFSFTRSYF MVEVPIPAEF VGFLKRILPG KHIAELYSSI GFYKHGKSEF
     YRALIDHLAN TDDRFVMAPG VRGMVMTVFT LPGFNTVFKL IKDRFSPIKS VNRANVIEKY
     RLVKSVDRVG RMADTQEFAD FRFPKAKFEP ECLAELLEVA PSTVEVQGDT VLVRHCWTER
     RMTPLNLYLE NASEQQVREA LEDYGLAIKQ LAAANIFPGD MLLKNFGVTR HGRVVFYDYD
     EISFLTEVNF RHIPPPRYPE DEMASEPWYS VGPNDVFPEE FPRFLFADLG QRRLFASLHG
     ELYDADYWKG LQDAIRQGKV IDVFPYRRKA DRN