Accession | TIGR00566 |
Name | trpG_papA |
Function | glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase |
Trusted Cutoff | 121.05 |
Domain Trusted Cutoff | 121.05 |
Noise Cutoff | 95.25 |
Domain Noise Cutoff | 95.25 |
Isology Type | subfamily |
HMM Length | 192 |
Gene Ontology Term | GO:0016884: carbon-nitrogen ligase activity, with glutamine as amido-N-donor molecular_function |
Author | Haft DH |
Entry Date | Oct 19 1999 4:31PM |
Last Modified | Jul 18 2011 12:08PM |
Comment | This HMM describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the PFAM HMM GATase. |
References | A2 hmmalign
DR PROSITE; PDOC00405; GATASE_TYPE_I;
DR PFAM; PF00117; GATase;
AL ClustalW |
Genome Property | GenProp0037: tryptophan biosynthesis from ribose-5-phosphate (HMM) |