Summary: Abhydrolase family
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This is the Wikipedia entry entitled "Alpha/beta hydrolase fold". More...
Alpha/beta hydrolase fold Edit Wikipedia article
| A bacterial lipase, one of this family members | |||||||||
| Identifiers | |||||||||
| Symbol | Abhydrolase_1 | ||||||||
| Pfam | PF00561 | ||||||||
| InterPro | IPR000073 | ||||||||
| SCOP | 1ede | ||||||||
| SUPERFAMILY | 1ede | ||||||||
| OPM superfamily | 135 | ||||||||
| OPM protein | 1qge | ||||||||
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In molecular biology, the alpha/beta hydrolase fold is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function.[1] The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices.[1][2] 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.
This catalytic domain is found in a very wide range of enzymes which do not share obvious sequence similarity. The alpha/beta hydrolase fold includes proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases.[3]
Contents |
[edit] Database
The ESTHER database provides a large collection of information about this family of proteins.[4]
[edit] Subfamilies
[edit] Human proteins containing this domain
ABHD10; ABHD11; ABHD12; ABHD12B; ABHD13; ABHD2; ABHD3; ABHD4; ABHD5; ABHD6; ABHD7; ABHD8; ABHD9; BAT5; BPHL; C20orf135; EPHX1; EPHX2; FAM108B1; LIPA; LIPF; LIPJ; LIPK; LIPM; LIPN; MEST; MGLL; PPME1; SERHL; SERHL2; SPG21; CES1; CES2
[edit] See also
- Serine hydrolase - an enzyme family that is composed largely of proteins with alpha-beta hydrolase folds
[edit] External links
[edit] References
- ^ a b Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., Sussman, J. L., Verschueren, K. H. G. & Goldman, A. (1992). "The alpha/beta hydrolase fold". Protein Eng. 5 (3): 197â211. doi:10.1093/protein/5.3.197. PMID 1409539.
- ^ Carr PD, Ollis DL (2009). "Alpha/beta hydrolase fold: an update". Protein Pept. Lett. 16 (10): 1137â48. PMID 19508187.
- ^ Nardini M, Dijkstra BW (December 1999). "Alpha/beta hydrolase fold enzymes: the family keeps growing". Curr. Opin. Struct. Biol. 9 (6): 732â7. doi:10.1016/S0959-440X(99)00037-8. PMID 10607665.
- ^ Renault L, Nègre V, Hotelier T, Cousin X, Marchot P, Chatonnet A (December 2005). "New friendly tools for users of ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins". Chem. Biol. Interact. 157-158: 339â43. doi:10.1016/j.cbi.2005.10.100. PMID 16297901.
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Abhydrolase family Provide feedback
This is a family of probable bacterial abhydrolases.
Internal database links
| Similarity to PfamA using HHSearch: | Abhydrolase_5 |
External database links
| PANDIT: | PF12715 |
| Pseudofam: | PF12715 |
| SYSTERS: | Abhydrolase_7 |
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 AB_hydrolase (CL0028), which contains the following 67 members:
Abhydro_lipase Abhydrolase_1 Abhydrolase_2 Abhydrolase_3 Abhydrolase_4 Abhydrolase_5 Abhydrolase_6 Abhydrolase_7 Abhydrolase_8 Acyl_transf_2 Arb2 AXE1 BAAT_C Chlorophyllase Chlorophyllase2 COesterase Cutinase DLH DUF1057 DUF1100 DUF1350 DUF1400 DUF1749 DUF2048 DUF2235 DUF2305 DUF2424 DUF2920 DUF2974 DUF3089 DUF3141 DUF3530 DUF452 DUF676 DUF726 DUF818 DUF829 DUF900 DUF915 EHN Esterase Esterase_phd FSH1 Hydrolase_4 LCAT 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 PhaC_N PHB_depo_C PhoPQ_related Ser_hydrolase Tannase Thioesterase UPF0227 VirJAlignments
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
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 (4) |
Full (102) |
Representative proteomes | NCBI (133) |
Meta (18) |
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| RP15 (4) |
RP35 (14) |
RP55 (17) |
RP75 (21) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
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 (4) |
Full (102) |
Representative proteomes | NCBI (133) |
Meta (18) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (4) |
RP35 (14) |
RP55 (17) |
RP75 (21) |
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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.
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 HMMER3.
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: | jcsg_3g8y |
| Previous IDs: | none |
| Type: | Family |
| Author: | Coggill P |
| Number in seed: | 4 |
| Number in full: | 102 |
| Average length of the domain: | 320.60 aa |
| Average identity of full alignment: | 36 % |
| Average coverage of the sequence by the domain: | 84.06 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 390 | ||||||||||||
| Family (HMM) version: | 2 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
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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 Abhydrolase_7 domain has been found. There are 7 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.
Loading structure mapping...

Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence