ACEK_BURL3
ID ACEK_BURL3 Reviewed; 605 AA.
AC Q39CF3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=Bcep18194_A6269;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB09863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000151; ABB09863.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041492972.1; NC_007510.1.
DR AlphaFoldDB; Q39CF3; -.
DR SMR; Q39CF3; -.
DR PRIDE; Q39CF3; -.
DR EnsemblBacteria; ABB09863; ABB09863; Bcep18194_A6269.
DR GeneID; 45096142; -.
DR KEGG; bur:Bcep18194_A6269; -.
DR PATRIC; fig|482957.22.peg.3286; -.
DR HOGENOM; CLU_033804_1_1_4; -.
DR OrthoDB; 245269at2; -.
DR Proteomes; UP000002705; Chromosome 1.
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..605
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000259147"
FT ACT_SITE 383
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 327..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 605 AA; 69925 MW; 2AE0F8CA247E2CEC CRC64;
MNHFPKLLSS QIGFDVAQTM LENFDRHYRI FREAAVEAKT LYEHGDWHGL QRLARERITS
YDDRVKECVE VLEDEYDAEN IDDEVWQQIK LHYIGLLTSH RQPECAETFF NSVCCKILHR
SYFSNDFIFV RPAISTEYLE NDEPAAKPTY RAYYPGTDGL ATTLERIVTN FQLEPAFDDL
PRDIGCVMQA IHDEFGHFDE APNFQIHVLS SLFFRNKSAY IVGRIINADR VLPFAVPIRH
VRPGVLSLDT VLLRRDQLMI IFGFSHSYFL VDMGVPSAYV DFLCTIMPGK PKAEIYTSVG
LQKQGKNLFY RDLLHHLSHS SDRFIIAPGI KGLVMLVFTL PSFPYVFKII KDHFPPPKET
TRAQIMEKYQ LVKRHDRLGR MADTLEYSSV ALPIARLDHA LVRELEKEVP SLLEYEDGNL
VIEHLYIERR MTPLNLYLQN GSDSDVEHGV KEYGNAVKEL MKANIFPGDM LYKNFGVTRH
GRVVFYDYDE IEYLTDCNVR RVPPPRNEED ELSGEPWYTV GPHDIFPETY GPFLLGDPRV
RDVFMKHHAD FFDPALWQAS KDKLIQGELP DFYPYDTALR FCTRYPARFG ATDQNDGAGD
AQRAA
