Accession | TIGR00134 |
Name | gatE_arch |
Function | glutamyl-tRNA(Gln) amidotransferase, subunit E |
Gene Symbol | gatE |
Trusted Cutoff | 319.55 |
Domain Trusted Cutoff | 319.55 |
Noise Cutoff | 223.40 |
Domain Noise Cutoff | 223.40 |
Isology Type | equivalog |
EC Number | 6.3.5.- |
HMM Length | 622 |
Mainrole Category | Protein synthesis |
Subrole Category | tRNA aminoacylation |
Gene Ontology Term | GO:0006424: glutamyl-tRNA aminoacylation biological_process |
| GO:0050567: glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity molecular_function |
Author | Haft DH |
Entry Date | Apr 20 1999 2:07PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This peptide is found only in the Archaea. It is paralogous to the gatB-encoded subunit of Glu-tRNA(Gln) amidotransferase. The GatABC system operates in many bacteria to convert Glu-tRNA(Gln) into Gln-tRNA(Gln). However, the homologous system in archaea instead converts Asp-tRNA(Asn) to Asn-tRNA(Asn). Glu-tRNA(Gln) is converted to Gln-tRNA(Gln) by a heterodimeric amidotransferase of GatE (this protein) and GatD.
The Archaea have an Asp-tRNA(Asn) amidotransferase instead of an Asp--tRNA ligase, but the genes have not been identified. It is likely that this protein replaces gatB in Asp-tRNA(Asn) amidotransferase but that both enzymes share gatA. |
References | DR PROSITE; PDOC00948;
DR PFAM; PF01162; PET112 family, C terminal region
RM 10993083
RT Domain-specific recruitment of amide amino acids for protein synthesis.
RA Tumbula DL, Becker HD, Chang WZ, Soll D.
RL Nature. 2000 Sep 7;407(6800):106-10.
DR HAMAP; MF_00588; 29 of 29 |
Genome Property | GenProp0258: tRNA aminoacylation (HMM) |
| GenProp0831: archaeal core gene set, exactly 1 per genome (HMM) |