ID ACEK_CITK8 Reviewed; 575 AA.
AC A8ANB7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 02-OCT-2024, entry version 89.
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=CKO_03904;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-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; CP000822; ABV14980.1; -; Genomic_DNA.
DR RefSeq; WP_012134674.1; NC_009792.1.
DR AlphaFoldDB; A8ANB7; -.
DR SMR; A8ANB7; -.
DR STRING; 290338.CKO_03904; -.
DR GeneID; 45137568; -.
DR KEGG; cko:CKO_03904; -.
DR HOGENOM; CLU_033804_1_1_6; -.
DR OrthoDB; 5287793at2; -.
DR Proteomes; UP000008148; 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: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..575
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_1000046552"
FT ACT_SITE 371
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 315..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 575 AA; 67234 MW; 3796706AC35CE5F5 CRC64;
MSRGLELLIA QTILQGFDAQ YGRFLEVTSG AQQRFEQADW HAVQQAMKSR IHLYDHHVGL
VVEQLRCITD GKSTDAAFLL RVKEHYTRLL PDYPRFEIAE SFFNSVYCRL FDHRSLTPER
LFIFSSQPER RFRTIPRPLA KDFFPDHGWE PLLTRILSDL PLRLPWQNKS RDIHYIIAHL
TETFGAEALH RSHLQVANEL FYRNKAAWLV GKLLTPAGTL PFLLPIHRTD EGELFVDTCL
TTTAEASIVF GFARSYFMVY APLPAALVEW LREILPGKTT AELYMAIGCQ KHAKTESYRE
YLLYLANSDE QFIEAPGIRG MVMLVFTLPG FDRVFKIIKD RFAPQKEMSA AHVRACYQLV
KEHDRVGRMA DTQEFENFVL EKRRIAPALM TLLRQEAPEK IIDLGDQIVI RHLYIERRMV
PLNIWLEQVE GQQLRDAIEE YGNAIRQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC
YMTEVNFRDI PQARYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF
RADYWRALQT RIREGHVEDV YAYRRKQRFC FRFAA
//
