ACEK_METPP
ID ACEK_METPP Reviewed; 618 AA.
AC A2SL82;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
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=Mpe_A3368;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM96321.1; -; Genomic_DNA.
DR RefSeq; WP_011830942.1; NC_008825.1.
DR AlphaFoldDB; A2SL82; -.
DR SMR; A2SL82; -.
DR STRING; 420662.Mpe_A3368; -.
DR PRIDE; A2SL82; -.
DR EnsemblBacteria; ABM96321; ABM96321; Mpe_A3368.
DR KEGG; mpt:Mpe_A3368; -.
DR eggNOG; COG4579; Bacteria.
DR HOGENOM; CLU_033804_1_1_4; -.
DR OMA; EPWYSVG; -.
DR OrthoDB; 245269at2; -.
DR Proteomes; UP000000366; 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..618
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000288289"
FT ACT_SITE 388
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 332..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 618 AA; 72031 MW; 125DFFC60B681FAD CRC64;
MAGSFVTTLN DPRAFDIAQA LLDGFNRHYK LFRQTSAEAK QRFEAADWHG QQRAQRERIE
FYDLRVDEAA ERLENEFRAS SLSEETWQQV KLYYIGLLIN HHQPELAETF FNSVTTKILH
RSYFRNDFIF VRPAVSTEYI ENEEPDSLPT YRAYYPSRPG SAEGLRETLL RIVDNYQLQR
EFEDLGRDID YVLQAFRNQF GDVKLSANFQ IQVLASLFFR NKGAYIVGKV INGFRETGFA
LPVLHNSREL LTIDTALFGE DELLLLFSFA RAYFLVDMEI PSAYVQFLRS LMPRKPRWEL
YNALGLQKQG KNQFYRDFLY HLRHSSDSFR IAPGIKGMVM LVFDLPSFPF VFKVIKDFYP
PQKDTTRELI QSKYQLVKTH DRVGRMADSL EYSNVAFPRQ RFEPELIEEI RHFCPSLLEE
EGDSLVLKHL YIERRMIPLN IYLQEATPEQ MKHAVIEYGN AIKDLVAANI FPGDMLWKNF
GVTRHGKVVF YDYDEIEYLT DCNFRKVPEP RTEEEEMSGD IWYSVGPKDV FPETFGPFLL
GNPTVREVFM QHHAELLDPA FWQGRKDRIA GGYVHDVFPY DPHKRFRRPL GLGFGSLDAE
AVSLHPASAT TQLGHNPI