ID ACEK_ALBFT Reviewed; 615 AA.
AC Q21RR4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 24-JUL-2024, entry version 92.
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=Rfer_3840;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-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}.
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DR EMBL; CP000267; ABD71539.1; -; Genomic_DNA.
DR RefSeq; WP_011466102.1; NC_007908.1.
DR AlphaFoldDB; Q21RR4; -.
DR SMR; Q21RR4; -.
DR STRING; 338969.Rfer_3840; -.
DR KEGG; rfr:Rfer_3840; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_4; -.
DR OrthoDB; 5287793at2; -.
DR Proteomes; UP000008332; Chromosome.
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..615
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000288297"
FT ACT_SITE 381
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 325..331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 615 AA; 71666 MW; 716ED446F0A86DEC CRC64;
MFPTRLDSSL AYDIAKAMMD GFNRHYRLFR TESARAKHRF ETADWHGQQR AQRDRIEFYD
LRVRECFMRL AREFKADEQP MEVWQQVKLH YIGLLVDHHQ PELAETFFNS VTTKILHHSY
FQNDFIFVRP AVSTEYIEND ESETSPTYRS YYPTHDSLAE VLVQMVLDFD LRCPFADLDS
DAARVQAAMV EQLGEVKLRA NFQLQVLSGL FFRNKGCYIV GKLINGFNEF PFALPVLYGR
AGQLVIDAVL FGEDDLLMLF SFARAYFMVD MEIPSAYVQY LRSMMPRKPR NEIYNALGLA
KQGKTLFYRD FLHHQRHSTD KFRIAPGIKG MVMLVFDLPS FPYVFKVIKD FYPPPKDTTR
EQIKAKYLLV KQHDRVGRMA DTLEYSEVGF PRARFDDELI AELEKFAPSQ LEISDRDGDG
RIEVIIKHVY IERRMIPLNI YLQEAFDAGG ANPDDTSPAA LRAREQIERG VIEYGNALKD
LVAANIFPGD MLWKNFGITR HGKVVFYDYD EIEYITDCNF RKVPQARNEE DEMSGEVWYR
VGPKDVFPET FAPFLLGNPF VREVFMKHHA ELLDAAFWQS HKERIQAGHV YDVFPYDQGK
RFHPEISDAQ VPSSI
//
