ACEK_PSEAE
ID ACEK_PSEAE Reviewed; 577 AA.
AC Q9I3W8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
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=PA1376;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG04765.1; -; Genomic_DNA.
DR PIR; D83473; D83473.
DR RefSeq; NP_250067.1; NC_002516.2.
DR RefSeq; WP_003112397.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I3W8; -.
DR SMR; Q9I3W8; -.
DR STRING; 287.DR97_417; -.
DR PaxDb; Q9I3W8; -.
DR PRIDE; Q9I3W8; -.
DR EnsemblBacteria; AAG04765; AAG04765; PA1376.
DR GeneID; 881156; -.
DR KEGG; pae:PA1376; -.
DR PATRIC; fig|208964.12.peg.1428; -.
DR PseudoCAP; PA1376; -.
DR HOGENOM; CLU_033804_1_1_6; -.
DR InParanoid; Q9I3W8; -.
DR OMA; EPWYSVG; -.
DR PhylomeDB; Q9I3W8; -.
DR BioCyc; PAER208964:G1FZ6-1402-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
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..577
FT /note="Isocitrate dehydrogenase kinase/phosphatase"
FT /id="PRO_0000057903"
FT ACT_SITE 374
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 318..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00747"
SQ SEQUENCE 577 AA; 66761 MW; B3E8A69981D5DC60 CRC64;
MVQSAPASEI AALILRGFDD YREQFREITD GARARFEQAQ WQEAQRASAQ RINLYEEKVA
ETVAGLRAGL ADSELLDVER WPIIKSAYIA QIDLRLDDEL AETWFNSIFC GLFSHDNISD
GTMFVHTTRP SLRAHARAPY TRTYRPGGDL RQALEKIFDD YRFDVPYDDR ERDLERIDAL
LHSNLPDWVC KDPDLAIELI GSVFYRNKGA YLVGRLFTPD EQWPLVFPLL HREDHGIQFD
TVITDEAEVS IIFSFTRSYF MVDVPVPAEL VAFLKRLLPG KHLAELYTSI GFYKQGKSEF
YRALINHLAT TDDRFVMAPG VRGMVMSVFT LPGFNTVFKI IKDRFNPSKS VDHATVIQKY
QLVKNHDRVG RLADTQQFAD FRFPVSKFEP ECLAELLEVA PSTVVMEGDV VLIRHCWTER
RMTPLNIYLE NASEAQTREA LNDYGLAIKQ LAAANIFPGD MLLKNFGVTR HGRVVFYDYD
EICYLTEVNF RYIPEPRFPE DEMSSEPWYS VGPNDVFPEE FPRFLFVDLN QRRLFAKLHG
NLYDAKYWQG LQEQIREGKV IDVFPYRRQE TPEQLLG
