1o1y

Protein Summary

The putative glutamine amido transferase (TM1158; NP_228964) from Thermotoga maritima belongs to a group of proteins present in all kingdoms of Life, having the type 1 glutamine amidotransferase (GATase1) domain with Cys88-His173-Glu175 catalytic triad in the glutaminase active site  (Pfam00117, cd01741). Glutamine amidotransferases transfer the amide nitrogen of glutamine to a variety of substrates (PubMed:9559052). The reaction is carried out by glutaminase and synthase subunits from the same or separate polypeptide chains (PubMed:8366040).

The 1o1y structure of glutaminase subunit (PubMed:14997577) described here, has a flavodoxin-like fold (SCOP sunid: 52171) with 3 layers, alpha/beta/alpha parallel beta-sheet of 5 strands, order 21345. TM1158 belongs to class I glutamine amidotransferases family (GAT; SCOP sunid: 52318).

Several proteins with structure similar to TM1158 have significant sequence similarity and contain all three catalytic residues (i.e. PDB structures: PDB:3l83 [Z=29], PDB:2a9v, chain A [Z=20], PDB:1wl8, chain A [Z=20], PDB:1qdl, chain B [Z=21], PDB:1i7q, chain B [Z=21], PDB:2h2w, chain A [Z=20], PDB:1i1q, chain B, PDB:1kxj, chain A, PDB:1q7r, chain A, PDB:1r9g, chain A, PDB:1ka9, chain H, PDB:1l9x, chain A, PDB:1gpm, chain A, PDB:1jvn, chain A, PDB:2abw, chain A, PDB:1bxr, chain B, 1vcmA , PDB:1s1m, chain A).  However TM1158 contains an additional alpha-helical "hairpin" close to the C-terminus (residues 176-210).

Ligand Summary

References