ID ACEK_PARP8 Reviewed; 602 AA.
AC B2JKI4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 24-JUL-2024, entry version 80.
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=Bphy_0180;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC69373.1; -; Genomic_DNA.
DR RefSeq; WP_012399602.1; NZ_CADFGH010000001.1.
DR AlphaFoldDB; B2JKI4; -.
DR SMR; B2JKI4; -.
DR STRING; 391038.Bphy_0180; -.
DR KEGG; bph:Bphy_0180; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_4; -.
DR OrthoDB; 5287793at2; -.
DR Proteomes; UP000001192; 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:0016208; F:AMP binding; IEA:TreeGrafter.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00747; AceK; 1.
DR InterPro; IPR046855; AceK_kinase.
DR InterPro; IPR046854; AceK_regulatory.
DR InterPro; IPR010452; Isocitrate_DH_AceK.
DR PANTHER; PTHR39559; -; 1.
DR PANTHER; PTHR39559:SF1; ISOCITRATE DEHYDROGENASE KINASE_PHOSPHATASE; 1.
DR Pfam; PF06315; AceK_kinase; 1.
DR Pfam; PF20423; AceK_regulatory; 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..602
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_1000133261"
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 602 AA; 69768 MW; 85980D507E54E44D CRC64;
MNHFPKLLSS QIGFDVAETL LAGFDRHYCI FREAAIRAKN LFEAADWHGL QKLARERITS
YDERVRECIA KLEDEYDAEN IDDDVWQQIK LHYIGLLTTH RQPECAETFF NSVCCHILHR
SYFNNDFIFV RPAISTEYIE NDEPAAKPTY RAYYPGKDGL AVTLERIVTN FQLNPPFENL
TRDVQCVIQA LRDNFGTFNE APNFQIHVLS SLFFRNKAAY IIGRIINGDM MLPFALPVHH
VKPGLLALDA LLCKRDQLLI IFSFAHSYFL VDMEVPSAYV EFLGSILHGK PKAEIYTSVG
LQKQGKNLFY RDLLRHLKHS SDRFIIAPGI KGMVMLVFTL PSFPYVFKLI KDAFPPPKET
TREQVVGKYQ LVKRHDRLGR MADTLEYSSV ALPLSRLDDA LIRELEKEAP SMLEYEGDNL
VIRHVYIERR MVPLNIFLQN GTDADIEHGI REYGNAVKEL MQANIFPGDM LYKNFGVTRH
GRVVFYDYDE IEYLTDCNVR AVPPPRNEED EMSGEPWYSV GPHDIFPETY NTFLLGDPRV
RESFLKHHAD FFDPALWQKQ KDYILRGELP DFYPYDRSLR FSIRYPERFA ADHVTAATER
AA
//
