Summary
alpha/beta hydrolase fold
This catalytic domain is found in a very wide range of enzymes.
Literature references
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Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A; , Protein Eng 1992;5:197-211.: The alpha/beta hydrolase fold PUBMED:1409539
InterPro entry IPR013094
The alpha/beta hydrolase fold PUBMED:1409539 is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices PUBMED:1409539. The enzymes are believed to have diverged from a common ancestor, preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best conserved structural features of the fold. Esterase (EST) from Pseudomonas putida is a member of the alpha/beta hydrolase fold superfamily of enzymes PUBMED:16321951.
In most of the family members the beta-strands are parallels, but some have an inversion of the first strands, which gives it an antiparallel orientation. The catalytic triad residues are presented on loops. One of these is the nucleophile elbow and is the most conserved feature of the fold. Some other members lack one or all of the catalytic residues. Some members are therefore inactive but others are involved in surface recognition. The ESTHER database PUBMED: gathers and annotates all the published information related to gene and protein sequences of this superfamily PUBMED:14681380.
This entry represents the catalytic domain fold-3 of alpha/beta hydrolase.
Clan
This family is a member of clan AB_hydrolase (CL0028), which contains the following 58 members:
Abhydrolase_1 Abhydrolase_2 Abhydrolase_3 Abhydrolase_4 Acyl_transf_2 Arb2 AXE1 BAAT_C Chlorophyllase COesterase Cutinase DLH DUF1023 DUF1057 DUF1100 DUF1234 DUF1350 DUF1400 DUF1749 DUF2048 DUF2305 DUF2424 DUF2920 DUF2974 DUF3141 DUF3530 DUF452 DUF676 DUF726 DUF818 DUF829 DUF900 DUF915 Esterase Esterase_phd FSH1 Hydrolase_4 LACT LIP Lipase Lipase_2 Lipase_3 Ndr PAF-AH_p_II Palm_thioest PE-PPE Peptidase_S10 Peptidase_S15 Peptidase_S28 Peptidase_S37 Peptidase_S9 PGAP1 PHB_depo_C PhoPQ_related Tannase Thioesterase UPF0227 VirJGene Ontology
| Molecular function | hydrolase activity (GO:0016787) |
| Biological process | metabolic process (GO:0008152) |
External database links
| PANDIT: | PF07859 |
| SYSTERS: | Abhydrolase_3 |
| External sites: | 1 |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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: | Pfam-B_100 (release 15.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 132 |
| Number in full: | 5385 |
| Average length of the domain: | 188.60 aa |
| Average identity of full alignment: | 21 % |
| Average coverage of the sequence by the domain: | 52.15 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 211 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There is 1 interaction for this family. More...
Abhydrolase_3Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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 Abhydrolase_3 domain has been found.
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