Summary
gamma-glutamylcysteine synthetase/glutamine synthetase clan
This clan represents a superfamily of carboxylate-amine/ammonia ligases [1] 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.
This clan contains 9 families and the total number of domains in the clan is 56026. The clan was built by A Bateman and J Pei.
Literature references
- Abbott JJ, Pei J, Ford JL, Qi Y, Grishin VN, Pitcher LA, Phillips MA, Grishin NV; , J Biol Chem. 2001;276:42099-42107.: Structure prediction and active site analysis of the metal binding determinants in gamma -glutamylcysteine synthetase. PUBMED:11527962 EPMC:11527962
Members
This clan contains the following 9 member families:
Amidoligase_2 ATP-gua_Ptrans DUF2126 GatB_N GCS GCS2 Gln-synt_C Glu_cys_ligase Pup_ligaseExternal database links
SCOP: | 55931 |
Domain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
Pfam family | Num. domains | Alignment |
---|---|---|
Gln-synt_C (PF00120) | 24915 (44.5%) | View |
GatB_N (PF02934) | 9382 (16.7%) | View |
GCS2 (PF04107) | 7350 (13.1%) | View |
ATP-gua_Ptrans (PF00217) | 4270 (7.6%) | View |
Pup_ligase (PF03136) | 2694 (4.8%) | View |
GCS (PF03074) | 2138 (3.8%) | View |
Amidoligase_2 (PF12224) | 1993 (3.6%) | View |
Glu_cys_ligase (PF04262) | 1830 (3.3%) | View |
DUF2126 (PF09899) | 1454 (2.6%) | View |
Total: 9 | Total: 56026 | Clan alignment |
Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.
Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
Tree controls
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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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 MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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