ACEK_BURM1
ID ACEK_BURM1 Reviewed; 605 AA.
AC A9AE52;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Bmul_0379, BMULJ_02875;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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}.
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DR EMBL; CP000868; ABX14074.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG44763.1; -; Genomic_DNA.
DR RefSeq; WP_012212617.1; NC_010804.1.
DR AlphaFoldDB; A9AE52; -.
DR SMR; A9AE52; -.
DR STRING; 395019.Bmul_0379; -.
DR EnsemblBacteria; BAG44763; BAG44763; BMULJ_02875.
DR KEGG; bmj:BMULJ_02875; -.
DR KEGG; bmu:Bmul_0379; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_4; -.
DR OMA; EPWYSVG; -.
DR Proteomes; UP000008815; 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..605
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_1000133260"
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; 70256 MW; DAC0BD1021138AD7 CRC64;
MNHFPKLLSS QIGFDVAQSM LEYFDRHYRI FREAAVEAKA LFERADWHGL QRLARERITS
YDERVQECVE VLQDEYDAES IDDEVWQQIK LHYIGLLTSH RQPECAETFF NSVCCKILHR
SYFNNDFIFV RPAISTEYLE NDEPAAKPTY RAYYPGTDGL AVTLERIVTN FQLEPPFEDL
ARDIACVMQA IHDEFGRFDE APNFQIHVLS SLFFRNKSAY IVGRIINADR VLPFAVPIRH
VRPGLLALDT VLLRRDLLQI IFSFSHSYFL VDMDVPSAYV DFLCTIMPGK PKAEIYTSVG
LQKQGKNLFY RDLLHHLSHS SDRFIVAPGI KGLVMLVFTL PSFPYVFKII KDHFPPPKET
TRRQIMEKYL LVKRHDRLGR MADTLEYSSV ALPLARLDHA LVRELEKEVP SLLEYEGDNL
VIKHLYIERR MTPLNLYLQN GTDAEVEHGV KEYGNAVKEL MKANIFPGDM LYKNFGVTRH
GRVVFYDYDE IEYLTDCNVR RVPPPRNEED ELSGEPWYTV GPHDIFPETY GPFLLGDPRV
RAAFLKHHAD FFDPALWQAS KDKLLQGELP DFFPYDASLR FCVRYPERFR ATDERAPARG
AQRAA
