ACEK_CUPNH
ID ACEK_CUPNH Reviewed; 613 AA.
AC Q8KLU8; Q0KFA1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=H16_A0168;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12193617; DOI=10.1128/jb.184.18.5018-5026.2002;
RA Kusian B., Sultemeyer D., Bowien B.;
RT "Carbonic anhydrase is essential for growth of Ralstonia eutropha at
RT ambient CO2 concentrations.";
RL J. Bacteriol. 184:5018-5026(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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; AJ310671; CAC80133.1; -; Genomic_DNA.
DR EMBL; AM260479; CAJ91320.1; -; Genomic_DNA.
DR RefSeq; WP_011614381.1; NZ_CP039287.1.
DR AlphaFoldDB; Q8KLU8; -.
DR SMR; Q8KLU8; -.
DR STRING; 381666.H16_A0168; -.
DR EnsemblBacteria; CAJ91320; CAJ91320; H16_A0168.
DR GeneID; 57642263; -.
DR KEGG; reh:H16_A0168; -.
DR PATRIC; fig|381666.6.peg.522; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_4; -.
DR OMA; EPWYSVG; -.
DR OrthoDB; 245269at2; -.
DR Proteomes; UP000008210; 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..613
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000057905"
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"
FT CONFLICT 275
FT /note="E -> K (in Ref. 1; CAC80133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 71480 MW; 2307038F15A1CD03 CRC64;
MSHFPKLLSS QIAFDVARTM LDGFDKHYRL FREVSHQAKL KFEAGDWHGL QQIQRDRIAF
YNERVRESSV ILEDEYDAEN IEDEIWQQIK LHYIGLLTNH HQPELAETFF NSVCTRILHR
SYFNNDFIFV RPAISTEYIE NEESPTRPTF RAYYPGSREG MAACFERVVH NFQLESPFED
LQRDIGYVVR AVSEHFGDLR IAPNFQVHTL SSLFFRNKSA FIIGRILNGD RTFPLAIPIV
HGPSGKLTLD TVLLKKEQLL ILFSFTHSYF MVDMEIPSAY VTFLRDIMPR KPRAEIYTSL
GLQKQGKNLF YRDFLHHLQH SSDKFIVAPG IRGLVMLVFT LPSYPYVFKV IKDFFPAPKE
TTRELVKSKY QLVKQHDRVG RMADTLEYSD VAFPLSRFDE ALVREFEQHA PSMIEYQRGK
DGGEEIVVRH VYIERRMTPL NIYLTEGTDE QVEHGVIEYG NAVKELIAAN IFPGDMLYKN
FGVTRHGRVV FYDYDEIEYL TDCNIRDVPQ PRNEEEEMSG EVWYTVRPHD IFPETFRTFL
LGDTRVRAAF LRHHADFFDP AMWQSHKDRL LAGHVHDFFA YHSSERFIHR YSEAGSAQGT
AAVPDPGPAR RVA
