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Phosphoenolpyruvate/pyruvate domain superfamily
SCOP classification
Superfamily statistics
Functional annotation
| General category | Metabolism |
| Detailed category | Energy |
Document: Function annotation of SCOP domain superfamilies
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
Worm Phenotype (WP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: WP annotation of SCOP domains
Yeast Phenotype (YP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: YP annotation of SCOP domains
Xenopus Anatomy (XA) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: XA annotation of SCOP domains
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
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 [
 11563914].
- C-terminal of pyruvate phosphate dikinase , which has a similar mode of substrate binding to pyruvate kinase [11790099].
- Phosphoenolpyruvate carboxylase ; this domain has additional helices [12467579].
- Phosphenolpyruvate mutase/Isocitrate lyase , where it forms a swapped dimer [11526312].
- 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 [7064730].
- Ketopantoate hydroxymethyltransferase PanB , where a C-terminal helix exchange is observed in some enzymes [12906829].
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InterPro database
PDBeMotif information about ligands, sequence and structure motifs
PDBeMotif resource
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Xenopus Anatomy (XA) · Enzyme Commission (EC) ]
Internal database links
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Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.
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Alignments of sequences to 42 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.
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Browse and view proteins in genomes which have
different domain combinations including a Phosphoenolpyruvate/pyruvate domain domain.
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Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
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Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.
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There are 42 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 inspected.
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Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Worm Phenotype (WP) · Yeast Phenotype (YP) · Xenopus Anatomy (XA) · Enzyme Commission (EC) · Internal database links ]
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