We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU00773
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00773
General rule information
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| Accession | PRU00773 |
| Dates | 08-APR-2009 (Created)
17-FEB-2023 (Last updated, Version 11) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51443; PCS |
Name | Phytochelatin synthase (PCS) domain |
| Function | Phytochelatins (PCs) are synthesized posttranslationally by the PC synthase (PCS) (EC 2.3.2.15), a gamma-glutamylcysteine (gamma-EC) transpeptidase. PC synthesis is proposed to have two distinct steps: (Step1) formation of gamma-EC concomitant with the cleavage of Gly from GSH; and (Step 2) transfer of the gamma-EC unit to an acceptor GSH molecule or an oligomeric PC peptide (PCn). |
| Scope(s) |
Eukaryota Bacteria Cyanobacteriota |
| Example(s) | Q2TE74; |
Propagated annotation
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Identifier, protein and gene names
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| case <FTGroup:1> | |
| Protein name | + AltName: Full=Glutathione gamma-glutamylcysteinyltransferase; EC=2.3.2.15; |
| end case | |
Comments
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| case <FTGroup:1> | |
| CATALYTIC ACTIVITY | Reaction=[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly + glycine; Xref=Rhea:RHEA:17917, Rhea:RHEA-COMP:12438, Rhea:RHEA- COMP:12439, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:131728; EC=2.3.2.15; |
| end case | |
| SIMILARITY | Belongs to the phytochelatin synthase family. |
Keywords
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| Transferase | |
| Acyltransferase | |
| end case | |
Gene Ontology
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| case <FTGroup:1> | |
| GO:0016756; Molecular function:glutathione gamma-glutamylcysteinyltransferase activity | |
| GO:0046938; Biological process:phytochelatin biosynthetic process | |
| GO:0016746; Molecular function:acyltransferase activity | |
Features
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| From: PS51443 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="Peptidase C83 #" | |||||||||
| ACT_SITE | 56 | 56 | C | 1 | ||||||||
| ACT_SITE | 168 | 168 | H | 1 | ||||||||
| ACT_SITE | 186 | 186 | D | 1 | ||||||||
Additional information
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| Size range | 210-231 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Eukaryota [8] All [ 8 ]
- Retrieve set of proteins with 3D structure for this domain