ACEK_BURCM
ID ACEK_BURCM Reviewed; 608 AA.
AC Q0BBE2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
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}; OrderedLocusNames=Bamb_2975;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) 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=ABI88531.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000440; ABI88531.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041491286.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BBE2; -.
DR SMR; Q0BBE2; -.
DR STRING; 339670.Bamb_2975; -.
DR EnsemblBacteria; ABI88531; ABI88531; Bamb_2975.
DR GeneID; 44693639; -.
DR KEGG; bam:Bamb_2975; -.
DR PATRIC; fig|339670.21.peg.1901; -.
DR eggNOG; COG4579; Bacteria.
DR Proteomes; UP000000662; 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..608
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000288284"
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 608 AA; 70231 MW; 0751B3C0EDA09CB6 CRC64;
MNHFPKLLSS QIGFDVAQTM LENFDRHYRI FREAAVDAKT LYERADWHGL QRLARERITS
YDDRVQECVE VLQDEYDAEN IDDEVWQQIK LHYIGLLTSH RQPECAETFF NSVCCKILHR
SYFSNDFIFV RPAISTEYLE NDEPAAKPTY RAYYPGTDGL AATLERIVTN FQLEPPFEDL
TRDIGCVMQA ITDEFGEFDA APNFQIHVLS SLFFRNKSAY IVGRIINADR VLPFAVPIRH
VRPGLLALDT LLLRRDLLQI IFSFSHSYFL VDMGVPSAYV EFLCTIMPGK PKAEIYTSVG
LQKQGKNLFY RDLLHHLSHS SDRFIIAPGI KGLVMLVFTL PSFPYVFKII KDHFPPPKET
TREQIMEKYQ LVKRHDRLGR MADTLEYSSV ALPISRLDHA LVRELEKEVP SLLEYEDGNL
VIKHLYIERR MIPLNLYLQN GTDAEIEHGV KEYGNAVKEL MKANIFPGDM LYKNFGVTRH
GRVVFYDYDE IEYLTDCNVR RVPPPRNEED ELSGEPWYTV GPHDIFPETY GPFLLGDPRV
RAVFMKHHAD FFEASLWQAS KDKLLQGELP DFFPYDVSLR FSVRYPDRFD ATPDAGDGDS
AGNAQRAA
