ECOLI:ACEK

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	aceK (ECO:0000255 with HAMAP-Rule:MF_00747)
Protein Name(s)	Isocitrate dehydrogenase kinase/phosphatase (ECO:0000255 with HAMAP-Rule:MF_00747) IDH kinase/phosphatase (ECO:0000255 with HAMAP-Rule:MF_00747) IDHK/P (ECO:0000255 with HAMAP-Rule:MF_00747)
External Links
UniProt	P11071
EMBL	M20714 M18974 U00006 U00096 AP009048 M22621 M63497
PIR	G65208
RefSeq	NP_418440.1 YP_492159.1
ProteinModelPortal	P11071
SMR	P11071
DIP	DIP-9041N
IntAct	P11071
MINT	MINT-1711235
STRING	511145.b4016
PptaseDB	P3D0409136
EnsemblBacteria	AAC76986 BAE78018
GeneID	12932473 944797
KEGG	ecj:Y75_p3903 eco:b4016
PATRIC	32123561
EchoBASE	EB0025
EcoGene	EG10026
eggNOG	COG4579
HOGENOM	HOG000247673
InParanoid	P11071
KO	K00906
OMA	EPWYSVG
OrthoDB	EOG6HQSJX
BioCyc	EcoCyc:ICITDEHASE-KIN-PHOSPHA ECOL316407:JW3976-MONOMER MetaCyc:ICITDEHASE-KIN-PHOSPHA
PRO	PR:P11071
Proteomes	UP000000318 UP000000625
Genevestigator	P11071
GO	GO:0005737 GO:0008772 GO:0016208 GO:0005524 GO:0004674 GO:0004722 GO:0016311 GO:0006006 GO:0006097 GO:0018105 GO:0050790 GO:0006099
HAMAP	MF_00747
InterPro	IPR010452
Pfam	PF06315
PIRSF	PIRSF000719
ProDom	PD043552

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0008772	[isocitrate dehydrogenase (NADP+)] kinase activity	PMID:10231385^[1]	ECO:0000314			F	Figures 1, 2, and 3.	complete CACAO 5411
involved_in	GO:0050790	regulation of catalytic activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10026 PANTHER:PTN002218346	P	Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10026 PANTHER:PTN002218346	P	Seeded From UniProt	complete
enables	GO:0016208	AMP binding	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10026 PANTHER:PTN002218346	F	Seeded From UniProt	complete
enables	GO:0008772	[isocitrate dehydrogenase (NADP+)] kinase activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10026 PANTHER:PTN002218346	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10026 PANTHER:PTN002218346	F	Seeded From UniProt	complete
enables	GO:0008772	[isocitrate dehydrogenase (NADP+)] kinase activity	PMID:6292732^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006099	tricarboxylic acid cycle	PMID:6292732^[3]	ECO:0000305	curator inference used in manual assertion	GO:0008772	P	Seeded From UniProt	complete
involved_in	GO:0006097	glyoxylate cycle	PMID:6292732^[3]	ECO:0000305	curator inference used in manual assertion	GO:0008772	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:6292732^[3]	ECO:0000305	curator inference used in manual assertion	GO:0008772	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:6292732^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0070262	peptidyl-serine dephosphorylation	PMID:6292732^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	PMID:6292732^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:3112144^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016208	AMP binding	PMID:20505668^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008772	[isocitrate dehydrogenase (NADP+)] kinase activity	PMID:6292732^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:8620880^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004722	protein serine/threonine phosphatase activity	PMID:8702587^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:3112144^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010452	C	Seeded From UniProt	complete
involved_in	GO:0006006	glucose metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010452	P	Seeded From UniProt	complete
enables	GO:0008772	[isocitrate dehydrogenase (NADP+)] kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010452	F	Seeded From UniProt	complete
enables	GO:0016791	phosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010452	F	Seeded From UniProt	complete
enables	GO:0008772	[isocitrate dehydrogenase (NADP+)] kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.11.5	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000099095	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000099095	C	Seeded From UniProt	complete
enables	GO:0008772	[isocitrate dehydrogenase (NADP+)] kinase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000099095	F	Seeded From UniProt	complete
enables	GO:0016788	hydrolase activity, acting on ester bonds	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000099095	F	Seeded From UniProt	complete
involved_in	GO:0006099	tricarboxylic acid cycle	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000099095	P	Seeded From UniProt	complete
involved_in	GO:0006097	glyoxylate cycle	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000099095	P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0004721	phosphoprotein phosphatase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0904	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
involved_in	GO:0006099	tricarboxylic acid cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0816	P	Seeded From UniProt	complete
involved_in	GO:0006097	glyoxylate cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0329	P	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Oudot, C et al. (1999) The isocitrate dehydrogenase kinase/phosphatase from Escherichia coli is highly sensitive to in-vitro oxidative conditions role of cysteine67 and cysteine108 in the formation of a disulfide-bonded homodimer. Eur. J. Biochem. 262 224-9 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 LaPorte, DC & Koshland, DE Jr (1982) A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle. Nature 300 458-60 PubMed GONUTS page
↑ ^4.0 ^4.1 Thorsness, PE & Koshland, DE Jr (1987) Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate. J. Biol. Chem. 262 10422-5 PubMed GONUTS page
↑ Zheng, J & Jia, Z (2010) Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Nature 465 961-5 PubMed GONUTS page
↑ Rittinger, K et al. (1996) Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues. Eur. J. Biochem. 237 247-54 PubMed GONUTS page
↑ Miller, SP et al. (1996) Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins. J. Biol. Chem. 271 19124-8 PubMed GONUTS page

[PMID:10231385-1] Oudot, C et al. (1999) The isocitrate dehydrogenase kinase/phosphatase from Escherichia coli is highly sensitive to in-vitro oxidative conditions role of cysteine67 and cysteine108 in the formation of a disulfide-bonded homodimer. Eur. J. Biochem. 262 224-9 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:6292732-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 ^3.7 LaPorte, DC & Koshland, DE Jr (1982) A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle. Nature 300 458-60 PubMed GONUTS page

[PMID:3112144-4] 4.0 ^4.1 Thorsness, PE & Koshland, DE Jr (1987) Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate. J. Biol. Chem. 262 10422-5 PubMed GONUTS page

[PMID:20505668-5] Zheng, J & Jia, Z (2010) Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Nature 465 961-5 PubMed GONUTS page

[PMID:8620880-6] Rittinger, K et al. (1996) Escherichia coli isocitrate dehydrogenase kinase/phosphatase. Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues. Eur. J. Biochem. 237 247-54 PubMed GONUTS page

[PMID:8702587-7] Miller, SP et al. (1996) Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins. J. Biol. Chem. 271 19124-8 PubMed GONUTS page

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ECOLI:ACEK

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