43  structures 104  species 3  interactions 292  sequences 34  architectures

Family: Lyase_8 (PF02278)

Summary

Polysaccharide lyase family 8, super-sandwich domain Add an annotation

This family consists of a group of secreted bacterial lyase enzymes EC:4.2.2.1 capable of acting on hyaluronan and chondroitin in the extracellular matrix of host tissues, contributing to the invasive capacity of the pathogen.


Literature references

  1. Farrell AM, Taylor D, Holland KT; , FEMS Microbiol Lett 1995;130:81-85.: Cloning, nucleotide sequence determination and expression of the Staphylococcus aureus hyaluronate lyase gene. PUBMED:7557301

  2. Fethiere J, Eggimann B, Cygler M; , J Mol Biol 1999;288:635-647.: Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes. PUBMED:10329169


InterPro entry IPR003159

Proteins containing this central domain consist of a group of secreted bacterial lyase enzymes capable of acting on a variety of substrates. One such enzyme is hyaluronate lyase, a Streptococcal surface enzyme that degrades hyaluronan and chondroitin, thereby helping to spread the bacteria throughout host tissues PUBMED:14523022. Hyaluronate lyase () is a four-domain enzyme containing an N-terminal carbohydrate-binding domain, a spacer domain, a catalytic domain, and a C-terminal domain that modulates access to the catalytic cleft of the enzyme. The central domain has a beta-sandwich topology, with 18 strands in two sheets. Other bacterial enzymes that display this structure include the central domain of chondroitin AC lyase () PUBMED:10329169, the central domain of xanthan lyase () PUBMED:12475987, and the third domain of chondroitin ABC lyase () PUBMED:12706721. This entry represents these domains of hyaluronate lyase, chondroitin AC lyase, xanthan lyase and chondroitin ABC lyase. This domain if almost always associated with the polysaccharide lyase family 8 C-terminal domain ().

Clan

This family is a member of clan Gal_mutarotase (CL0103), which contains the following 5 members:

Aldose_epim Bgal_small_N Glyco_hydro_38C Glyco_hydro_65N Lyase_8

Gene Ontology

External database links

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...

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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.

Pfam alignments:
Full length sequences

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.

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. 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 View help on the curation process

Seed source: Pfam-B_4840 (release 5.2)
Previous IDs: none
Type: Family
Author: Mian N, Bateman A, Griffiths-Jones SR
Number in seed: 5
Number in full: 292
Average length of the domain: 260.20 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 28.26 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.0 20.0
Trusted cut-off 23.3 20.4
Noise cut-off 19.4 18.9
Model length: 269
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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The tree shows the occurrence of this domain across different species. More...

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Interactions

There are 3 interactions for this family. More...

Lyase_8_C Lyase_catalyt Lyase_8_N

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 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 Lyase_8 domain has been found.

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