Summary: Glutamate-cysteine ligase family 2(GCS2)
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Glutamate-cysteine ligase family 2(GCS2) Provide feedback
Also known as gamma-glutamylcysteine synthetase and gamma-ECS ( EC:188.8.131.52). This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver  discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes, from an ancestral bacterial enzyme. They also state that Arabidopsis thaliana gamma-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast and Escherichia coli homologues. In plants, there are separate cytosolic and chloroplast forms of the enzyme.
May MJ, Leaver CJ; , Proc Natl Acad Sci U S A 1994;91:10059-10063.: Arabidopsis thaliana gamma-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast, and Escherichia coli homologs. PUBMED:7937837 EPMC:7937837
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR006336
Also known as gamma-glutamylcysteine synthetase and gamma-ECS (EC). This enzyme catalyses the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver [PUBMED:7937837] discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes, from an ancestral bacterial enzyme. They also state that Arabidopsis thaliana (Mouse-ear cress) gamma-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast and Escherichia coli homologues. In plants, there are separate cytosolic and chloroplast forms of the enzyme.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||glutamate-cysteine ligase activity (GO:0004357)|
|Biological process||glutathione biosynthetic process (GO:0006750)|
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This clan represents a superfamily of carboxylate-amine/ammonia ligases  that includes Gamma-Glutamylcysteine synthetase (gamma-GCS) and glutamine synthetase (GS). Gamma-Glutamylcysteine synthetase (gamma-GCS) catalyses the first step in the de novo biosynthesis of glutathione.
The clan contains the following 9 members:Amidoligase_2 ATP-gua_Ptrans COOH-NH2_lig DUF2126 GCS GCS2 Gln-synt_C Glu_cys_ligase Pup_ligase
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Curation and family details
|Author:||Kerrison ND, Finn RD|
|Number in seed:||12|
|Number in full:||2189|
|Average length of the domain:||275.90 aa|
|Average identity of full alignment:||24 %|
|Average coverage of the sequence by the domain:||68.31 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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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 GCS2 domain has been found. There are 13 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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