ACEK_PSEPK
ID ACEK_PSEPK Reviewed; 571 AA.
AC Q88EA1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=PP_4565;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70138.1; -; Genomic_DNA.
DR RefSeq; NP_746674.1; NC_002947.4.
DR RefSeq; WP_010955236.1; NC_002947.4.
DR AlphaFoldDB; Q88EA1; -.
DR SMR; Q88EA1; -.
DR STRING; 160488.PP_4565; -.
DR EnsemblBacteria; AAN70138; AAN70138; PP_4565.
DR KEGG; ppu:PP_4565; -.
DR PATRIC; fig|160488.4.peg.4868; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_6; -.
DR OMA; EPWYSVG; -.
DR PhylomeDB; Q88EA1; -.
DR BioCyc; PPUT160488:G1G01-4873-MON; -.
DR Proteomes; UP000000556; 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..571
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000057904"
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 571 AA; 65954 MW; 0A94EE44E65C1298 CRC64;
MSQPWPAVEI ARMILAGFDD YRDHFQRITL GARQRFEQAR WQDIQQAAAA RINLYEEKVA
EVNGWLRQAF AAEVLLDVEQ WPLVKNAYIH LIDPRLDDEL AETWYNSLFC SLFSHDLISD
GCMFIHTTRP SMRGRERAAQ TRTYRLDGSL RNLLRAVFAD YPFDMPYGDL EGDLARLEEQ
LRECLPDWVC KDPALAVELF VPVLYRNKGA YLVGRLYNSD EQWPLVIPLL HREGHGIEAD
ALITDEAEVS IIFSFTRSYF MADVPVPAEF VNFLKRILPG KHIAELYTSI GFYKQGKSEF
YRALINHLAS SDDRFVMAPG VRGMVMSVFT LPGFNTVFKI IKDRFSPSKT VDRATVIDKY
RLVKSVDRVG RMADTQEFAD FRFPRSKFEP DCLAELLEVA PSTVALEGDT VLIRHCWTER
RMTPLNLYLE QATEGQVLEA LEDYGLAIKQ LAAANIFPGD MLLKNFGVTR HGRVVFYDYD
EISFLTEVNF RHIPPPRYPE DEMSGEPWYS IGPHDVFPEE FPPFLFADMG QRRLFSRLHG
ELYDADYWKG LQAAIREGKV IDVFPYRRKA R
