Protein profile

PA1376

bifunctional isocitrate dehydrogenase kinase/phosphatase

Genome: NC_002516.2

Gene: aceK PA1376 Structure source: AlphaFold UniProt Q9I3W8
Amino acids 577
Annotations 12
Features 10
PDB binders 0
Druggability 0.372

Overview

Basic information about this protein and its source genome.

Accession
PA1376
Gene
aceK PA1376
Status
annotated
Amino acids
577
Structure source
AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.372
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 10 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

10
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0008772 Catalysis of the reaction: ATP + L-seryl-[isocitrate dehydrogenase] = ADP + H+ + O-phospho-L-seryl-[isocitrate dehydrogenase].
  • GO:0016208 Binding to AMP, adenosine monophosphate.
  • GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
  • GO:0004721 Catalysis of the reaction: a phosphoprotein + H2O = a protein + phosphate. Together with protein kinases, these enzymes control the state of phosphorylation of cellular proteins and thereby provide an important mechanism for regulating cellular activity.
  • GO:0004674 Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
  • GO:0006006 The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
  • GO:0006097 A modification of the TCA cycle occurring in some plants and microorganisms, in which isocitrate is cleaved to glyoxylate and succinate. Glyoxylate can then react with acetyl-CoA to form malate.
  • GO:0006099 A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.
  • GO:0016791 Catalysis of the hydrolysis of a phosphoric monoester, releasing a phosphate.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records
Show feature table
Start End DB Term Name
2 573 Hamap MF_00747 Isocitrate dehydrogenase kinase/phosphatase [aceK].
2 573 InterPro IPR010452 Isocitrate dehydrogenase kinasephosphatase
1 577 PIRSF PIRSF000719 AceK
1 577 InterPro IPR010452 Isocitrate dehydrogenase kinasephosphatase
11 311 Pfam PF20423 Isocitrate dehydrogenase kinase/phosphatase (AceK), regulatory domain
11 311 InterPro IPR046854 Isocitrate dehydrogenase kinase/phosphatase (AceK), regulatory domain
1 575 PANTHER PTHR39559 -
1 575 InterPro IPR010452 Isocitrate dehydrogenase kinasephosphatase
313 567 Pfam PF06315 Isocitrate dehydrogenase kinase/phosphatase (AceK) kinase domain
313 567 InterPro IPR046855 Isocitrate dehydrogenase kinase/phosphatase (AceK), kinase domain

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA1376
AlphaFold full sequence Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
3 0.372
2 0.325
4 0.211