ACEK_RALSO
ID ACEK_RALSO Reviewed; 608 AA.
AC Q8Y2Q7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=RSc0278;
GN ORFNames=RS03245;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD13806.1; -; Genomic_DNA.
DR RefSeq; WP_011000245.1; NC_003295.1.
DR AlphaFoldDB; Q8Y2Q7; -.
DR SMR; Q8Y2Q7; -.
DR STRING; 267608.RSc0278; -.
DR PRIDE; Q8Y2Q7; -.
DR EnsemblBacteria; CAD13806; CAD13806; RSc0278.
DR GeneID; 60499784; -.
DR KEGG; rso:RSc0278; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_4; -.
DR OMA; EPWYSVG; -.
DR Proteomes; UP000001436; 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: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..608
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000057906"
FT ACT_SITE 384
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 328..334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 608 AA; 70553 MW; A7300AF83E114901 CRC64;
MSHFPKLLSS QIAFDVARTM LDGFDKHYRL FREVSVRAKA LFEAGDWQGL QQLQRDRIAY
YDERVREASV ILEDEYDAEN IDDEIWRQIK LHFIGLLTNH HQPECAETFF NSVCTRILHR
SYFNNDFIFL RPAISTEYIE NEESPTKPTY RAYYPGSREG LGGCLERIVH NFQLDAPFED
LPRDIGYVVR AVGEHFGDFR IAPNFQIHVL SSLFFRNTAA YIIGRVINGD KTYPLAVPIM
RGADGQLRLD TVLLRPEQLL ILFSFTHSYF MVDMEIPSAY VTFLRDLMPR KPRAEIYTSL
GLQKQGKNLF YRDFLHHLQH SSDKFIIAPG IKGLVMLVFT LPSYPYVFKV IKDYFPPPKE
TTRELIKSKY QLVKQHDRVG RMADTLEYSD VAFPLSRFDD ALIKELEKHA PSMVEYQRGA
DGSDEIVIRH VYIERRMTPL NIWLHEGTDA QVEHGIIEYG NAIKELIAAN IFPGDMLYKN
FGVTRHGRVV FYDYDEIEYL TDCNVRDVPQ PRNEEEEMSG EVWYSVGPHD IFPQTYGTFL
LGDPRVREAF LRHHADFFDP AMWQAHKARL LSGQTHDFYA YDASERFVNR YGDSAPGNAA
TPLRRAAA
