Summary: Pyruvate kinase, barrel domain
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Pyruvate kinase, barrel domain Provide feedback
This domain of the is actually a small beta-barrel domain nested within a larger TIM barrel. The active site is found in a cleft between the two domains.
Larsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH; , Arch Biochem Biophys 1997;345:199-206.: Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution. PUBMED:9308890 EPMC:9308890
Internal database links
|Similarity to PfamA using HHSearch:||HpcH_HpaI|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015793
The enzyme, which is found in all living organisms, requires both magnesium and potassium ions for its activity. In vertebrates, there are four tissue-specific isozymes: L (liver), R (red cells), M1 (muscle, heart and brain), and M2 (early foetal tissue). In plants, PK exists as cytoplasmic and plastid isozymes, while most bacteria and lower eukaryotes have one form, except in certain bacteria, such as Escherichia coli, that have two isozymes. All isozymes appear to be tetramers of identical subunits of ~500 residues.
PK helps control the rate of glycolysis, along with phosphofructokinase (INTERPRO) and hexokinase (INTERPRO). PK possesses allosteric sites for numerous effectors, yet the isozymes respond differently, in keeping with their different tissue distributions [PUBMED:12798932]. The activity of L-type (liver) PK is increased by fructose-1,6-bisphosphate (F1,6BP) and lowered by ATP and alanine (gluconeogenic precursor), therefore when glucose levels are high, glycolysis is promoted, and when levels are low, gluconeogenesis is promoted. L-type PK is also hormonally regulated, being activated by insulin and inhibited by glucagon, which covalently modifies the PK enzyme. M1-type (muscle, brain) PK is inhibited by ATP, but F1,6BP and alanine have no effect, which correlates with the function of muscle and brain, as opposed to the liver.
The structure of several pyruvate kinases from various organisms have been determined [PUBMED:11960989, PUBMED:10751408]. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a beta/alpha-barrel domain, a beta-barrel domain (inserted within the beta/alpha-barrel domain), and a 3-layer alpha/beta/alpha sandwich domain.
This entry represents the two barrel domains, the beta/alpha-barrel, and the beta-barrel inserted within it.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||potassium ion binding (GO:0030955)|
|magnesium ion binding (GO:0000287)|
|pyruvate kinase activity (GO:0004743)|
|Biological process||glycolysis (GO:0006096)|
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This superfamily consists of a number of TIM barrel domains found in enzymes such as pyruvate kinase, malate synthase and citrate lyase.
The clan contains the following 10 members:C-C_Bond_Lyase HpcH_HpaI ICL Malate_synthase Pantoate_transf PEP-utilizers_C PEP_mutase PEPcase PEPcase_2 PK
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Curation and family details
|Author:||Finn RD, Griffiths-Jones SR|
|Number in seed:||13|
|Number in full:||7047|
|Average length of the domain:||326.30 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||68.66 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PK domain has been found. There are 229 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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