ACEK_ECOL5
ID ACEK_ECOL5 Reviewed; 574 AA.
AC Q0TA53;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=ECP_4226;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000247; ABG72176.1; -; Genomic_DNA.
DR RefSeq; WP_001137237.1; NC_008253.1.
DR AlphaFoldDB; Q0TA53; -.
DR SMR; Q0TA53; -.
DR STRING; 362663.ECP_4226; -.
DR EnsemblBacteria; ABG72176; ABG72176; ECP_4226.
DR KEGG; ecp:ECP_4226; -.
DR HOGENOM; CLU_033804_1_1_6; -.
DR OMA; EPWYSVG; -.
DR Proteomes; UP000009182; 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; Serine/threonine-protein kinase;
KW Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..574
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000259151"
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 574 AA; 67206 MW; 8285CBDABE00D7EB CRC64;
MPRGLELLIA QTILQGFDAQ YGRFLEVTSG AQQRFEQADW HAVQQAMKNR IHLYDHHVGL
VVEQLRCITN GQSTDAAFLL RVKEHYTRLL PDYPRFEIAE SFFNSVYCRL FDHRSLTPER
LFIFSSQPER RFRTIPRPLA KDFHPDHGWE SLLMRVISDL PLRLRWQNKS RDIHYIVRHL
TETLGTDNLA ESHLQVANEL FYRNKAAWLV GKLITPSGTL PFLLPIHQTD DGELFIDTCL
TTTAEASIVF GFARSYFMVY APLPAALVEW LREILPGKTT AELYMAIGCQ KHAKTESYRE
YLVYLQGCNE QFIEAPGIRG MVMLVFTLPG FDRVFKVIKD RFAPQKEMSA AHVRACYQLV
KEHDRVGRMA DTQEFENFVL EKRHISPALM ELLLQEAAEK ITDLGEQIVI RHLYIERRMV
PLNIWLEQVE GQQLRDAIEE YGNAIRQLAA ANIFPGDMLF KNFGVTRHGR VVFYDYDEIC
YMTEVNFRDI PLPRYPEDEL ASEPWYSVSP GDVFPEEFRH WLCADPRIGP LFEEMHADLF
RADYWRALQN RIREGHVEDV YAYRRRQRFS VRFV