4  structures 86  species 1  interaction 147  sequences 3  architectures

Family: Phytochelatin (PF05023)

Summary

Phytochelatin synthase Add an annotation

Phytochelatin synthase is the enzyme responsible for the synthesis of heavy-metal-binding peptides (phytochelatins) from glutathione and related thiols [2]. The crystal structure of a member of this family shows it to possess a papain fold [3]. The enzyme catalyses the deglycination of a GSH donor molecule [3]. The enzyme contains a catalytic triad of cysteine, histidine and aspartate residues.


Literature references

  1. Clemens S, Kim EJ, Neumann D, Schroeder JI; , EMBO J 1999;18:3325-3333.: Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast. PUBMED:10369673

  2. Vatamaniuk OK, Bucher EA, Ward JT, Rea PA; , Trends Biotechnol 2002;20:61-64.: Worms take the 'phyto' out of 'phytochelatins'. PUBMED:11814595

  3. Vivares D, Arnoux P, Pignol D; , Proc Natl Acad Sci U S A. 2005;102:18848-18853.: A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis. PUBMED:16339904


InterPro entry IPR007719

This entry represents plant phytochelatin synthases (also known as glutathione gamma-glutamylcysteinyltransferase; ), which is involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. This enzyme is required for detoxification of heavy metals such as cadmium and arsenate. The N-terminal region of phytochelatin synthase contains the active site, as well as four highly conserved cysteine residues that appear to play an important role in heavy-metal-induced phytochelatin catalysis. The C-terminal region is rich in cysteines, and may act as a metal sensor, whereby the Cys residues bind cadmium ions to bring them into closer proximity and transferring them to the activation site in the N-terminal catalytic domain PUBMED:18270423. The C-terminal region displays homology to the functional domains of metallothionein and metallochaperone.

Clan

This family is a member of clan Peptidase_CA (CL0125), which contains the following 44 members:

Acetyltransf_2 Amidase_5 CHAP DUF1175 DUF1287 DUF1460 DUF553 DUF830 DUF920 NLPC_P60 OTU Peptidase_C1 Peptidase_C10 Peptidase_C12 Peptidase_C16 Peptidase_C1_2 Peptidase_C2 Peptidase_C21 Peptidase_C23 Peptidase_C27 Peptidase_C28 Peptidase_C31 Peptidase_C32 Peptidase_C33 Peptidase_C34 Peptidase_C36 Peptidase_C39 Peptidase_C42 Peptidase_C47 Peptidase_C54 Peptidase_C58 Peptidase_C6 Peptidase_C65 Peptidase_C7 Peptidase_C70 Peptidase_C71 Peptidase_C78 Peptidase_C8 Peptidase_C9 Phytochelatin Rad4 Transglut_core UCH Viral_protease

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_9299 (release 7.6)
Previous IDs: none
Type: Domain
Author: Wood V, Rawlings ND
Number in seed: 20
Number in full: 147
Average length of the domain: 205.40 aa
Average identity of full alignment: 39 %
Average coverage of the sequence by the domain: 58.96 %

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 23.8 23.8
Trusted cut-off 23.8 24.0
Noise cut-off 23.4 23.7
Model length: 213
Family (HMM) version: 7
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

Phytochelatin

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 Phytochelatin domain has been found.

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