SUPERFAMILY 1.73 HMM library and genome assignments server


Phosphoenolpyruvate/pyruvate domain superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a/b) [ 51349] (141)
  Mainly parallel beta sheets (beta-alpha-beta units)
Fold:   TIM beta/alpha-barrel [ 51350] (33)
  contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
the first seven superfamilies have similar phosphate-binding sites
Superfamily:   Phosphoenolpyruvate/pyruvate domain [ 51621] (6)
Families:   Pyruvate kinase [ 51622]
  Pyruvate phosphate dikinase, C-terminal domain [ 51629]
  Phosphoenolpyruvate carboxylase [ 51632]
  Phosphoenolpyruvate mutase/Isocitrate lyase-like [ 88704] (3)
  forms a swapped dimer
  HpcH/HpaI aldolase [ 51638] (3)
  forms a swapped dimer; contains a PK-type metal-binding site
  Ketopantoate hydroxymethyltransferase PanB [ 89503]


InterPro annotation
Cross references IPR015813 SSF51621 Protein matches
Abstract

Pyruvate kinase controls the exit from the glysolysis pathway, catalysing the transfer of phosphate from phosphooenolpyruvate (PEP) to ADP. Mammalian pyruvate kinase is a homotetramer, where each polypeptide subunit consists of four domains: N-terminal, A domain, B domain and C-terminal. Activation of the enzyme is believed to occur via the clamping down of the B domain onto the A domain to dehydrate the active site cleft. The N- and C-terminal domains are situated at inter-subunit contact sites, and could be involved in assembly and communication within the complex. The N-terminal domain has a TIM beta/alpha-barrel structure. Homologous TIM-barrel domains are found in the following proteins:

  • N-terminal of pyruvate kinase , which is interrupted by an all-beta domain [PubMed11563914].
  • C-terminal of pyruvate phosphate dikinase , which has a similar mode of substrate binding to pyruvate kinase [PubMed11790099].
  • Phosphoenolpyruvate carboxylase ; this domain has additional helices [PubMed12467579].
  • Phosphenolpyruvate mutase/Isocitrate lyase , where it forms a swapped dimer [PubMed11526312].
  • HpcH/HpaI aldolases, such as the beta subunit of citrate lyase, where it forms a swapped dimer, and contains a pyruvate kinase-type metal binding site [PubMed7064730].
  • Ketopantoate hydroxymethyltransferase PanB , where a C-terminal helix exchange is observed in some enzymes [PubMed12906829].

InterPro database

Functional annotation
General category Metabolism
Detailed category Energy

Function annotation of SCOP domain superfamilies

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Internal database links

The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level. Click on the 'Genome Assignments' icon above to view the genome assignments for this superfamily.


Alignments of sequences to

Alignments of sequences to 23 models in this superfamily are available by clicking on the superfamily level 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequences may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own.


It is possible to browse and view the proteins in the genomes which have different combinations of domains including a Phosphoenolpyruvate/pyruvate domain domain. Click on the 'Domain Combinations' icon.


To view the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom click on the 'TaxViz' icon above. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Undirected domain occurrence networks are available for all superfamilies. Nodes in these networks represent genomes. Connections between nodes represent the presence of domain architectures, which contain the superfamily of interest, in both genomes.

There are 23 hidden Markov models representing the Phosphoenolpyruvate/pyruvate domain superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be viewed by clicking on the icon above.


Jump to [ Top of page · SCOP classification · InterPro annotation · Functional annotation · Internal database links ]