2 experimentally studied proteins
38 sequences in Swiss-Prot
3,723 unique sequences in UniRef100
The Glutamyl-tRNA amido-transferase subunit D family, a group of achaeal enzymes that also contain the Class 1 asparaginase domain
Could also have L-asparaginase activity and high affinity to L-asparagine
| Fam ? Class - Clan - Family | Alt ? Alternative historical name / classification | AN ? UniProt accession number | Name ? UniProt entry name, only given here for Swiss-Prot entries | EC | Organism | Cell-Loc | AAs | Structure | PDB | Km i for Asn [mM] | Vmax i for Asn [μmol/min/mg] | Kcat i for Asn [s-1] | |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 1-4-12 | - | O26802 | GATD_METTH | 6.3.5.- | Methanothermobacter thermautotrophicus | - | 435 | Hetero tetramer i Has additional domain. | 2D6F | - | - | - | |
| 1-4-12 | - | Q9V0T9 | GATD_PYRAB | 6.3.5.- | Pyrococcus abyssi | - | 438 | Hetero tetramer i Has additional domain. | 1ZQ1 | - | - | - |
| Fam ? Class - Clan - Family | Alt ? Alternative historical name / classification | AN ? UniProt accession number | Name ? UniProt entry name, only given here for Swiss-Prot entries | EC | Organism | Cell-Loc | AAs | Structure | PDB | Km i for Asn [mM] | Vmax i for Asn [μmol/min/mg] | Kcat i for Asn [s-1] | |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 1-4-12 | - | Q9Y9T8 | GATD_AERPE | 6.3.5.- | Aeropyrum pernix | - | 427 | - | - | - | - | - | |
| 1-4-12 | - | O29380 | GATD_ARCFU | 6.3.5.- | Archaeoglobus fulgidus | - | 418 | - | - | - | - | - | |
| 1-4-12 | - | B0R6H4 | GATD_HALS3 | 6.3.5.- | Halobacterium salinarum | - | 427 | - | - | - | - | - | |
| 1-4-12 | - | Q9HP20 | GATD_HALSA | 6.3.5.- | Halobacterium salinarum | - | 427 | - | - | - | - | - | |
| 1-4-12 | - | Q18GL3 | GATD_HALWD | 6.3.5.- | Haloquadratum walsbyi | - | 442 | - | - | - | - | - | |
| 1-4-12 | - | Q8TR66 | GATD_METAC | 6.3.5.- | Methanosarcina acetivorans | - | 424 | - | - | - | - | - | |
| 1-4-12 | - | Q46GJ6 | GATD_METBF | 6.3.5.- | Methanosarcina barkeri | - | 424 | - | - | - | - | - | |
| 1-4-12 | - | Q12X65 | GATD_METBU | 6.3.5.- | Methanococcoides burtonii | - | 415 | - | - | - | - | - | |
| 1-4-12 | - | Q60331 | GATD_METJA | 6.3.5.- | Methanocaldococcus jannaschii | - | 417 | - | - | - | - | - | |
| 1-4-12 | - | Q8TV84 | GATD_METKA | 6.3.5.- | Methanopyrus kandleri | - | 458 | - | - | - | - | - | |
| 1-4-12 | - | A4FWR5 | GATD_METM5 | 6.3.5.- | Methanococcus maripaludis | - | 418 | - | - | - | - | - | |
| 1-4-12 | - | A9AA46 | GATD_METM6 | 6.3.5.- | Methanococcus maripaludis | - | 418 | - | - | - | - | - | |
| 1-4-12 | - | A6VGK5 | GATD_METM7 | 6.3.5.- | Methanococcus maripaludis | - | 418 | - | - | - | - | - | |
| 1-4-12 | - | Q8PUM7 | GATD_METMA | 6.3.5.- | Methanosarcina mazei | - | 425 | - | - | - | - | - | |
| 1-4-12 | - | P61400 | GATD_METMP | 6.3.5.- | Methanococcus maripaludis | - | 418 | - | - | - | - | - | |
| 1-4-12 | - | A5UK11 | GATD_METS3 | 6.3.5.- | Methanobrevibacter smithii | - | 436 | - | - | - | - | - | |
| 1-4-12 | - | A4YHH3 | GATD_METS5 | 6.3.5.- | Metallosphaera sedula | - | 439 | - | - | - | - | - | |
| 1-4-12 | - | Q2NEH1 | GATD_METST | 6.3.5.- | Methanosphaera stadtmanae | - | 438 | - | - | - | - | - | |
| 1-4-12 | - | O26802 | GATD_METTH | 6.3.5.- | Methanothermobacter thermautotrophicus | - | 435 | Hetero tetramer i Has additional domain. | 2D6F | - | - | - | |
| 1-4-12 | - | A6UPR4 | GATD_METVS | 6.3.5.- | Methanococcus vannielii | - | 426 | - | - | - | - | - | |
| 1-4-12 | - | P61401 | GATD_NANEQ | 6.3.5.- | Nanoarchaeum equitans | - | 392 | - | - | - | - | - | |
| 1-4-12 | - | Q9V0T9 | GATD_PYRAB | 6.3.5.- | Pyrococcus abyssi | - | 438 | Hetero tetramer i Has additional domain. | 1ZQ1 | - | - | - | |
| 1-4-12 | - | Q8ZY04 | GATD_PYRAE | 6.3.5.- | Pyrobaculum aerophilum | - | 417 | - | - | - | - | - | |
| 1-4-12 | - | Q8U0X0 | GATD_PYRFU | 6.3.5.- | Pyrococcus furiosus | - | 438 | - | - | - | - | - | |
| 1-4-12 | - | O59132 | GATD_PYRHO | 6.3.5.- | Pyrococcus horikoshii | - | 438 | - | - | - | - | - | |
| 1-4-12 | - | Q97ZH5 | GATD_SACS2 | 6.3.5.- | Saccharolobus solfataricus | - | 444 | - | - | - | - | - | |
| 1-4-12 | - | Q4J955 | GATD_SULAC | 6.3.5.- | Sulfolobus acidocaldarius | - | 446 | - | - | - | - | - | |
| 1-4-12 | - | C3N5E7 | GATD_SULIA | 6.3.5.- | Sulfolobus islandicus | - | 445 | - | - | - | - | - | |
| 1-4-12 | - | C4KH13 | GATD_SULIK | 6.3.5.- | Sulfolobus islandicus | - | 445 | - | - | - | - | - | |
| 1-4-12 | - | C3MPS1 | GATD_SULIL | 6.3.5.- | Sulfolobus islandicus | - | 445 | - | - | - | - | - | |
| 1-4-12 | - | C3MYR5 | GATD_SULIM | 6.3.5.- | Sulfolobus islandicus | - | 445 | - | - | - | - | - | |
| 1-4-12 | - | C3NHQ2 | GATD_SULIN | 6.3.5.- | Sulfolobus islandicus | - | 445 | - | - | - | - | - | |
| 1-4-12 | - | C3NE01 | GATD_SULIY | 6.3.5.- | Sulfolobus islandicus | - | 445 | - | - | - | - | - | |
| 1-4-12 | - | Q971W5 | GATD_SULTO | 6.3.5.- | Sulfurisphaera tokodaii | - | 448 | - | - | - | - | - | |
| 1-4-12 | - | Q9HJJ5 | GATD_THEAC | 6.3.5.- | Thermoplasma acidophilum | - | 409 | - | - | - | - | - | |
| 1-4-12 | - | Q5JI77 | GATD_THEKO | 6.3.5.- | Thermococcus kodakarensis | - | 440 | - | - | - | - | - | |
| 1-4-12 | - | A1RX40 | GATD_THEPD | 6.3.5.- | Thermofilum pendens | - | 451 | - | - | - | - | - | |
| 1-4-12 | - | Q979L8 | GATD_THEVO | 6.3.5.- | Thermoplasma volcanium | - | 406 | - | - | - | - | - |
Clan 4 is an interesting clan of bacterial and archaeal L-asparaginases. Some sequences display characteristics of both "type I" and "type II" L-asparaginases and some are structurally unique.
Sequences in Family 12 are called glutamyl-tRNA(Gln) amidotransferase subunit D. These archaeal enzymes catalyse the transamidation from L-glutamine to L-glutamyl-tRNA(Gln) to form L-glutaminyl-tRNA(Gln). The BLAST search results revealed some bacteria carry the gene coding this protein, too. In addition to the L-asparaginase domain, they contain ~100 amino acid N-terminal residues. Together with glutamyl-tRNA(Gln) amidotransferase subunit E, they form the mature hetero dimer. L-Asparagine can also be the substrate of this enzyme, acting as the amide donor.
