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4  structures 1678  species 2  interactions 1779  sequences 6  architectures

Family: GSH-S_ATP (PF02955)

Summary: Prokaryotic glutathione synthetase, ATP-grasp domain

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This is the Wikipedia entry entitled "Glutathione synthetase". More...

Glutathione synthetase Edit Wikipedia article

glutathione synthetase
Identifiers
Symbol GSS
Entrez 2937
HUGO 4624
OMIM 601002
RefSeq NM_000178
UniProt P48637
Other data
Locus Chr. 20 q11.2
Eukaryotic glutathione synthase
PDB 2hgs EBI.jpg
human glutathione synthetase
Identifiers
Symbol GSH_synthase
Pfam PF03199
Pfam clan CL0483
InterPro IPR004887
SCOP 2hgs
SUPERFAMILY 2hgs
Eukaryotic glutathione synthase, ATP binding domain
PDB 2hgs EBI.jpg
human glutathione synthetase
Identifiers
Symbol GSH_synth_ATP
Pfam PF03917
InterPro IPR005615
SCOP 1m0t
SUPERFAMILY 1m0t
Prokaryotic glutathione synthetase, N-terminal domain
PDB 1gsh EBI.jpg
structure of escherichia coli glutathione synthetase at ph 7.5
Identifiers
Symbol GSH-S_N
Pfam PF02951
InterPro IPR004215
SCOP 1glv
SUPERFAMILY 1glv
Prokaryotic glutathione synthetase, ATP-grasp domain
PDB 1gsh EBI.jpg
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

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]

See also[edit]

References[edit]

  1. ^ NjÃ¥lsson R, Norgren S (2005). "Physiological and pathological aspects of GSH metabolism.". Acta Paediatr 94 (2): 132–7. doi:10.1080/08035250410025285. PMID 15981742. 
  2. ^ 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): 3204–13. doi:10.1093/emboj/18.12.3204. PMC 1171401. PMID 10369661. 

External links[edit]


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

Prokaryotic glutathione synthetase, ATP-grasp domain Provide feedback

No Pfam abstract.

Literature references

  1. 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


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004218

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 is the ATP-binding domain of the enzyme.

Gene Ontology

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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
(37)
Full
(1779)
Representative proteomes NCBI
(2863)
Meta
(2533)
RP15
(103)
RP35
(240)
RP55
(337)
RP75
(426)
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Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(37)
Full
(1779)
Representative proteomes NCBI
(2863)
Meta
(2533)
RP15
(103)
RP35
(240)
RP55
(337)
RP75
(426)
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
(37)
Full
(1779)
Representative proteomes NCBI
(2863)
Meta
(2533)
RP15
(103)
RP35
(240)
RP55
(337)
RP75
(426)
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.

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'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: Structural domain
Previous IDs: none
Type: Domain
Author: Griffiths-Jones SR, Bateman A
Number in seed: 37
Number in full: 1779
Average length of the domain: 171.60 aa
Average identity of full alignment: 52 %
Average coverage of the sequence by the domain: 54.80 %

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 20.5 20.5
Trusted cut-off 20.5 20.5
Noise cut-off 20.4 20.4
Model length: 174
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

GSH-S_N GSH-S_ATP

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_ATP 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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