ID   ACEK_ECO8A              Reviewed;         578 AA.
AC   B7M7S1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=ECIAI1_4237;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAR00987.1; -; Genomic_DNA.
DR   RefSeq; WP_001137214.1; NC_011741.1.
DR   AlphaFoldDB; B7M7S1; -.
DR   SMR; B7M7S1; -.
DR   GeneID; 66672073; -.
DR   KEGG; ecr:ECIAI1_4237; -.
DR   HOGENOM; CLU_033804_1_1_6; -.
DR   OMA; EPWYSVG; -.
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..578
FT                   /note="Isocitrate dehydrogenase kinase/phosphatase"
FT                   /id="PRO_1000133266"
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   578 AA;  67671 MW;  B939E96E97AC91A9 CRC64;
     MPRGLELLIA QTILQGFDAQ YGRFLEVTSG AQQRFEQADW HAVQQAMKNR IHLYDHHVGL
     VVEQLRCITN GQSTDAAFLL RVKEHYTRLL PDYPRFEIAE SFFNSVYCRL FDHRSLTPER
     LFIFSSQPER RFRTIPRPLA KDFHPDHGWE SLLMRVISDL PLRLRWQNKS RDIHYIIRHL
     TETLGTDNLA ESHLQVANEL FYRNKAAWLV GKLITPSGTL PFLLPIHQTD DGELFIDTCL
     TTTAEASIVF GFARSYFMVY APLPAALVEW LREILPGKTT AELYMAIGCQ KHAKTESYRE
     YLVYLQGCNE QFIEAPGIRG MVMLVFTLPG FDRVFKVIKD KFAPQKEMSA AHVRACYQLV
     KEHDRVGRMA DTQEFENFVL EKRHISPALM ELLLQEAAEK ITDLGEQIVI RHLYIERRMV
     PLNIWLEQVE GQQLRDAIEE YGNAIRQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC
     YMTEVNFRDI PPPRYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF
     RADYWRALQN RIREGHVEDV YAYRRRQRFS VRYGEMLF