Summary: Enolase, N-terminal domain
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This is the Wikipedia entry entitled "Enolase". More...
Enolase Edit Wikipedia article
Enolase is a protein that acts as an enzyme to catalyze one of the final reaction in glycolisis.
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Enolase, N-terminal domain Provide feedback
No Pfam abstract.
Internal database links
SCOOP: | Enolase_C |
External database links
HOMSTRAD: | enolase |
PRINTS: | PR00148 |
PROSITE: | PDOC00148 |
SCOP: | 1els |
This tab holds annotation information from the InterPro database.
InterPro entry IPR020811
Enolase (2-phospho-D-glycerate hydrolase) is an essential, homodimeric enzyme that catalyses the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways [ PUBMED:1859865 , PUBMED:1840492 ]. The reaction is facilitated by the presence of metal ions [ PUBMED:8605183 ]. In vertebrates, there are 3 different, tissue-specific isoenzymes, designated alpha, beta and gamma. Alpha is present in most tissues, beta is localised in muscle tissue, and gamma is found only in nervous tissue. The functional enzyme exists as a dimer of any 2 isoforms. In immature organs and in adult liver, it is usually an alpha homodimer, in adult skeletal muscle, a beta homodimer, and in adult neurons, a gamma homodimer. In developing muscle, it is usually an alpha/beta heterodimer, and in the developing nervous system, an alpha/gamma heterodimer [ PUBMED:3390159 ]. The tissue specific forms display minor kinetic differences. Tau-crystallin, one of the major lens proteins in some fish, reptiles and birds, has been shown [ PUBMED:3589669 ] to be evolutionary related to enolase.
Neuron-specific enolase is released in a variety of neurological diseases, such as multiple sclerosis and after seizures or acute stroke. Several tumour cells have also been found positive for neuron-specific enolase. Beta-enolase deficiency is associated with glycogenosis type XIII defect.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Enolase_N (CL0227), which has the following description:
This domain is found at the N-terminus of the catalytic Tim barrel-like domain in enolase and other enzymes.
The clan contains the following 4 members:
Enolase_like_N Enolase_N MAAL_N MR_MLE_NAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (632) |
Full (13645) |
Representative proteomes | UniProt (55445) |
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RP15 (1948) |
RP35 (6291) |
RP55 (12848) |
RP75 (20933) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
— not available.
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
Seed (632) |
Full (13645) |
Representative proteomes | UniProt (55445) |
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RP15 (1948) |
RP35 (6291) |
RP55 (12848) |
RP75 (20933) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Prosite |
Previous IDs: | enolase_N; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Sonnhammer ELL |
Number in seed: | 632 |
Number in full: | 13645 |
Average length of the domain: | 125.2 aa |
Average identity of full alignment: | 59 % |
Average coverage of the sequence by the domain: | 29.94 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 131 | ||||||||||||
Family (HMM) version: | 19 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
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 Enolase_N domain has been found. There are 220 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 sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.