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175  structures 3408  species 4  interactions 9019  sequences 58  architectures

Family: Abhydrolase_1 (PF00561)

Summary: alpha/beta hydrolase fold

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Alpha/beta hydrolase fold". More...

Alpha/beta hydrolase fold Edit Wikipedia article

1qge opm.gif
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

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 beta strands connected by 6 alpha 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]

Database[edit]

The ESTHER database provides a large collection of information about this family of proteins.[4]

Subfamilies[edit]

Human proteins containing this domain[edit]

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

See also[edit]

  • Serine hydrolase - an enzyme family that is composed largely of proteins with alpha-beta hydrolase folds

External links[edit]

References[edit]

  1. ^ 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): 197–211. doi:10.1093/protein/5.3.197. PMID 1409539. 
  2. ^ Carr PD, Ollis DL (2009). "Alpha/beta hydrolase fold: an update". Protein Pept. Lett. 16 (10): 1137–48. PMID 19508187. 
  3. ^ Nardini M, Dijkstra BW (December 1999). "Alpha/beta hydrolase fold enzymes: the family keeps growing". Curr. Opin. Struct. Biol. 9 (6): 732–7. doi:10.1016/S0959-440X(99)00037-8. PMID 10607665. 
  4. ^ 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: 339–43. 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.

alpha/beta hydrolase fold Provide feedback

This catalytic domain is found in a very wide range of enzymes.

Literature references

  1. 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 EPMC:1409539


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000073

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:14681380] gathers and annotates all the published information related to gene and protein sequences of this superfamily [PUBMED:14681380].

This entry represents fold-1 of alpha/beta hydrolase.

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

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
(48)
Full
(9019)
Representative proteomes NCBI
(47284)
Meta
(15466)
RP15
(897)
RP35
(1658)
RP55
(2474)
RP75
(3041)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(48)
Full
(9019)
Representative proteomes NCBI
(47284)
Meta
(15466)
RP15
(897)
RP35
(1658)
RP55
(2474)
RP75
(3041)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

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
(48)
Full
(9019)
Representative proteomes NCBI
(47284)
Meta
(15466)
RP15
(897)
RP35
(1658)
RP55
(2474)
RP75
(3041)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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.

Pfam alignments:

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 View help on the curation process

Seed source: MRC-LMB Genome group
Previous IDs: abhydrolase;
Type: Domain
Author: Bateman A
Number in seed: 48
Number in full: 9019
Average length of the domain: 242.40 aa
Average identity of full alignment: 13 %
Average coverage of the sequence by the domain: 59.97 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.1 24.1
Trusted cut-off 24.1 24.1
Noise cut-off 24.0 24.0
Model length: 230
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 4 interactions for this family. More...

Abhydrolase_1 Abhydro_lipase Hydrolase EHN

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_1 domain has been found. There are 175 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.

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