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

19-345 (Pyruvate kinase)

Relief mechanism

PTM, Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

3 structures for P00549

Entry ID Method Resolution Chain Position Source
1A3W X-ray 300 A A/B 1-500 PDB
1A3X X-ray 300 A A/B 1-500 PDB
AF-P00549-F1 Predicted AlphaFoldDB

No variants for P00549

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P00549

No associated diseases with P00549

3 regional properties for P00549

Type Name Position InterPro Accession
domain Pyruvate kinase, barrel 19 - 345 IPR015793
domain Pyruvate kinase, C-terminal 380 - 497 IPR015795
active_site Pyruvate kinase, active site 235 - 247 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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

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

4 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.
pyruvate metabolic process The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.

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
P11979 PKM Pyruvate kinase PKM Felis catus (Cat) (Felis silvestris catus) SS
P00548 PKM Pyruvate kinase PKM Gallus gallus (Chicken) 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
MSRLERLTSL NVVAGSDLRR TSIIGTIGPK TNNPETLVAL RKAGLNIVRM NFSHGSYEYH
70 80 90 100 110 120
KSVIDNARKS EELYPGRPLA IALDTKGPEI RTGTTTNDVD YPIPPNHEMI FTTDDKYAKA
130 140 150 160 170 180
CDDKIMYVDY KNITKVISAG RIIYVDDGVL SFQVLEVVDD KTLKVKALNA GKICSHKGVN
190 200 210 220 230 240
LPGTDVDLPA LSEKDKEDLR FGVKNGVHMV FASFIRTAND VLTIREVLGE QGKDVKIIVK
250 260 270 280 290 300
IENQQGVNNF DEILKVTDGV MVARGDLGIE IPAPEVLAVQ KKLIAKSNLA GKPVICATQM
310 320 330 340 350 360
LESMTYNPRP TRAEVSDVGN AILDGADCVM LSGETAKGNY PINAVTTMAE TAVIAEQAIA
370 380 390 400 410 420
YLPNYDDMRN CTPKPTSTTE TVAASAVAAV FEQKAKAIIV LSTSGTTPRL VSKYRPNCPI
430 440 450 460 470 480
ILVTRCPRAA RFSHLYRGVF PFVFEKEPVS DWTDDVEARI NFGIEKAKEF GILKKGDTYV
490
SIQGFKAGAG HSNTLQVSTV