Summary: Prokaryotic glutathione synthetase, N-terminal domain
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Glutathione synthetase Edit Wikipedia article
| glutathione synthetase | |
|---|---|
| Identifiers | |
| Symbol | GSS |
| Entrez | 2937 |
| HUGO | 4624 |
| OMIM | 601002 |
| RefSeq | NM_000178 |
| UniProt | P48637 |
| Other data | |
| EC number | 6.3.2.3 |
| Locus | Chr. 20 q11.2 |
| Eukaryotic glutathione synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| human glutathione synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | GSH_synthase | ||||||||
| Pfam | PF03199 | ||||||||
| Pfam clan | CL0483 | ||||||||
| InterPro | IPR004887 | ||||||||
| SCOP | 2hgs | ||||||||
| SUPERFAMILY | 2hgs | ||||||||
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| Eukaryotic glutathione synthase, ATP binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| human glutathione synthetase | |||||||||
| Identifiers | |||||||||
| Symbol | GSH_synth_ATP | ||||||||
| Pfam | PF03917 | ||||||||
| InterPro | IPR005615 | ||||||||
| SCOP | 1m0t | ||||||||
| SUPERFAMILY | 1m0t | ||||||||
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| Prokaryotic glutathione synthetase, N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| structure of escherichia coli glutathione synthetase at ph 7.5 | |||||||||
| Identifiers | |||||||||
| Symbol | GSH-S_N | ||||||||
| Pfam | PF02951 | ||||||||
| InterPro | IPR004215 | ||||||||
| SCOP | 1glv | ||||||||
| SUPERFAMILY | 1glv | ||||||||
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| Prokaryotic glutathione synthetase, ATP-grasp domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| structure of escherichia coli glutathione synthetase at ph 7.5 | |||||||||
| Identifiers | |||||||||
| Symbol | GSH-S_ATP | ||||||||
| Pfam | PF02955 | ||||||||
| Pfam clan | CL0179 | ||||||||
| InterPro | IPR004218 | ||||||||
| SCOP | 1glv | ||||||||
| SUPERFAMILY | 1glv | ||||||||
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Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione.[1]
In eukaryotes, this is a homodimeric enzyme. In humans, defects in GSS are inherited in an autosomal recessive way and are the cause of severe metabolic acidosis, 5-oxoprolinuria, and increased rate of haemolysis and defective function of the central nervous system. The substrate-binding domain has a 3-layer alpha/beta/alpha structure.[2]
[edit] See also
[edit] References
- ^ NjÃ¥lsson R, Norgren S (2005). "Physiological and pathological aspects of GSH metabolism.". Acta Paediatr 94 (2): 132â7. doi:10.1080/08035250410025285. PMID 15981742.
- ^ Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW (June 1999). "Molecular basis of glutathione synthetase deficiency and a rare gene permutation event". EMBO J. 18 (12): 3204â13. doi:10.1093/emboj/18.12.3204. PMC 1171401. PMID 10369661. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1171401/.
[edit] External links
- Glutathione Synthetase at the US National Library of Medicine Medical Subject Headings (MeSH)
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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.
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No Pfam abstract.
Literature references
-
Yamaguchi H, Kato H, Hata Y, Nishioka T, Kimura A, Oda J, Katsube Y; , J Mol Biol 1993;229:1083-1100.: Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution. PUBMED:8445637 EPMC:8445637
External database links
| PANDIT: | PF02951 |
| Pseudofam: | PF02951 |
| SCOP: | 1glv |
| SYSTERS: | GSH-S_N |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004215
Prokaryotic glutathione synthetase EC (glutathione synthase) catalyses the conversion of gamma-L-glutamyl-L-cysteine and glycine to orthophosphate and glutathione in the presence of ATP. This is the second step in glutathione biosynthesis. The enzyme is inhibited by 7,8-dihydrofolate, methotrexate and trimethoprim. This domain is the N terminus of the enzyme.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | glutathione synthase activity (GO:0004363) |
| Biological process | glutathione biosynthetic process (GO:0006750) |
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 (155) |
Full (1672) |
Representative proteomes | NCBI (1136) |
Meta (1521) |
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| RP15 (89) |
RP35 (217) |
RP55 (308) |
RP75 (395) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
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Format an alignment
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 (155) |
Full (1672) |
Representative proteomes | NCBI (1136) |
Meta (1521) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (89) |
RP35 (217) |
RP55 (308) |
RP75 (395) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
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
| Seed source: | Structural domain |
| Previous IDs: | GTS_N; |
| Type: | Domain |
| Author: | Griffiths-Jones SR |
| Number in seed: | 155 |
| Number in full: | 1672 |
| Average length of the domain: | 119.20 aa |
| Average identity of full alignment: | 46 % |
| Average coverage of the sequence by the domain: | 37.80 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 119 | ||||||||||||
| Family (HMM) version: | 9 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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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 GSH-S_N domain has been found. There are 4 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence