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6  structures 167  species 0  interactions 240  sequences 21  architectures

Family: Polysacc_lyase (PF14099)

Summary: Polysaccharide lyase

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

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

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.

Polysaccharide lyase Provide feedback

This family includes heparin lyase I, EC:4.2.2.7. Heparin lyase I depolymerises heparin by cleaving the glycosidic linkage next to an iduronic acid moiety [1,2]. The structure of heparin lyase I consists of a beta-jelly roll domain with a long, deep substrate-binding groove and an unusual thumb domain containing many basic residues extending from the main body of the enzyme [2]. This family also includes glucuronan lyase, EC:4.2.2.14 [3]. The structure glucuronan lyase is a beta-jelly roll [4].

Literature references

  1. Ernst S, Venkataraman G, Winkler S, Godavarti R, Langer R, Cooney CL, Sasisekharan R;, Biochem J. 1996;315:589-597.: Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum. PUBMED:8615834 EPMC:8615834

  2. Han YH, Garron ML, Kim HY, Kim WS, Zhang Z, Ryu KS, Shaya D, Xiao Z, Cheong C, Kim YS, Linhardt RJ, Jeon YH, Cygler M;, J Biol Chem. 2009;284:34019-34027.: Structural snapshots of heparin depolymerization by heparin lyase I. PUBMED:19801541 EPMC:19801541

  3. Konno N, Igarashi K, Habu N, Samejima M, Isogai A;, Appl Environ Microbiol. 2009;75:101-107.: Cloning of the Trichoderma reesei cDNA encoding a glucuronan lyase belonging to a novel polysaccharide lyase family. PUBMED:18978091 EPMC:18978091

  4. Konno N, Ishida T, Igarashi K, Fushinobu S, Habu N, Samejima M, Isogai A;, FEBS Lett. 2009;583:1323-1326.: Crystal structure of polysaccharide lyase family 20 endo-beta-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei. PUBMED:19306878 EPMC:19306878


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR025975

This family includes heparin lyase I (EC). Heparin lyase I depolymerises heparin by cleaving the glycosidic linkage next to an iduronic acid moiety [PUBMED:8615834, PUBMED:19801541]. The structure of heparin lyase I consists of a beta-jelly roll domain with a long, deep substrate-binding groove and an unusual thumb domain containing many basic residues extending from the main body of the enzyme [PUBMED:19801541]. This family also includes glucuronan lyase, (EC) [PUBMED:18978091]. The structure glucuronan lyase is a beta-jelly roll [PUBMED:19306878].

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...

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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
(54)
Full
(240)
Representative proteomes NCBI
(254)
Meta
(933)
RP15
(41)
RP35
(77)
RP55
(100)
RP75
(118)
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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
(54)
Full
(240)
Representative proteomes NCBI
(254)
Meta
(933)
RP15
(41)
RP35
(77)
RP55
(100)
RP75
(118)
Alignment:
Format:
Order:
Sequence:
Gaps:
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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
(54)
Full
(240)
Representative proteomes NCBI
(254)
Meta
(933)
RP15
(41)
RP35
(77)
RP55
(100)
RP75
(118)
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.

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: Jackhmmer:Q7UP23
Previous IDs: none
Type: Family
Author: Eberhardt R
Number in seed: 54
Number in full: 240
Average length of the domain: 233.50 aa
Average identity of full alignment: 15 %
Average coverage of the sequence by the domain: 63.76 %

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 29.9 29.9
Trusted cut-off 29.9 30.3
Noise cut-off 29.8 29.8
Model length: 224
Family (HMM) version: 1
Download: download the raw HMM for this family

Species distribution

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This 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...

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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 Polysacc_lyase domain has been found. There are 6 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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