Descriptions

Pyruvate kinase M2 (PKM2) plays a vital role in glycolysis, and it catalyzes the conversion of phosphoenolpyruvate to pyruvate with the production of ATP in the final reaction of glycolysis. PKM2 provides an in vivo growth advantage in cancer cells. Pyruvate Kinase isozymes type PKM1, PKL, and PKR exist in unstable and high-activity tetramer forms, whereas PKM2 is found in both a highly active tetramer form and a low-activity dimer form. The switch between dimer and tetramer is allosterically modulated by the binding of ligands such as amino acids and metabolic intermediates to the regulatory C-terminal domain. Post-translational modifications at specific residues relieve this inhibition, allowing metabolic flux.

Autoinhibitory domains (AIDs)

Target domain

42-374 (Pyruvate kinase)

Relief mechanism

PTM, Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P00548

Entry ID Method Resolution Chain Position Source
AF-P00548-F1 Predicted AlphaFoldDB

No variants for P00548

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P00548

No associated diseases with P00548

3 regional properties for P00548

Type Name Position InterPro Accession
domain Pyruvate kinase, barrel 42 - 374 IPR015793
domain Pyruvate kinase, C-terminal 409 - 527 IPR015795
active_site Pyruvate kinase, active site 264 - 276 IPR018209

Functions

Description
EC Number 2.7.1.40 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
magnesium ion binding Binding to a magnesium (Mg) ion.
potassium ion binding Binding to a potassium ion (K+).
pyruvate kinase activity Catalysis of the reaction

3 GO annotations of biological process

Name Definition
cellular response to insulin stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
glycolytic process The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P52489 PYK2 Pyruvate kinase 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P00549 CDC19 Pyruvate kinase 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P11979 PKM Pyruvate kinase PKM Felis catus (Cat) (Felis silvestris catus) SS
Q29536 PKLR Pyruvate kinase PKLR Canis lupus familiaris (Dog) (Canis familiaris) SS
O62619 PyK Pyruvate kinase Drosophila melanogaster (Fruit fly) SS
P30613 PKLR Pyruvate kinase PKLR Homo sapiens (Human) SS
P14618 PKM Pyruvate kinase PKM Homo sapiens (Human) EV
P52480 Pkm Pyruvate kinase PKM Mus musculus (Mouse) SS
P53657 Pklr Pyruvate kinase PKLR Mus musculus (Mouse) SS
P12928 Pklr Pyruvate kinase PKLR Rattus norvegicus (Rat) SS
P11980 Pkm Pyruvate kinase PKM Rattus norvegicus (Rat) SS
Q9LIK0 PKP1 Plastidial pyruvate kinase 1, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSKHHDAGTA FIQTQQLHAA MADTFLEHMC RLDIDSEPTI ARNTGIICTI GPASRSVDKL
70 80 90 100 110 120
KEMIKSGMNV ARLNFSHGTH EYHEGTIKNV REATESFASD PITYRPVAIA LDTKGPEIRT
130 140 150 160 170 180
GLIKGSGTAE VELKKGAALK VTLDNAFMEN CDENVLWVDY KNLIKVIDVG SKIYVDDGLI
190 200 210 220 230 240
SLLVKEKGKD FVMTEVENGG MLGSKKGVNL PGAAVDLPAV SEKDIQDLKF GVEQNVDMVF
250 260 270 280 290 300
ASFIRKAADV HAVRKVLGEK GKHIKIISKI ENHEGVRRFD EIMEASDGIM VARGDLGIEI
310 320 330 340 350 360
PAEKVFLAQK MMIGRCNRAG KPIICATQML ESMIKKPRPT RAEGSDVANA VLDGADCIML
370 380 390 400 410 420
SGETAKGDYP LEAVRMQHAI AREAEAAMFH RQQFEEILRH SVHHREPADA MAAGAVEASF
430 440 450 460 470 480
KCLAAALIVM TESGRSAHLV SRYRPRAPII AVTRNDQTAR QAHLYRGVFP VLCKQPAHDA
490 500 510 520
WAEDVDLRVN LGMNVGKARG FFKTGDLVIV LTGWRPGSGY TNTMRVVPVP