| Accession | TIGR00262 |
| Name | trpA |
| Function | tryptophan synthase, alpha subunit |
| Gene Symbol | trpA |
| Trusted Cutoff | 102.35 |
| Domain Trusted Cutoff | 102.35 |
| Noise Cutoff | 100.35 |
| Domain Noise Cutoff | 100.35 |
| Isology Type | equivalog |
| EC Number | 4.2.1.20 |
| HMM Length | 256 |
| Mainrole Category | Amino acid biosynthesis |
| Subrole Category | Aromatic amino acid family |
| Gene Ontology Term | GO:0000162: tryptophan biosynthetic process biological_process |
| | GO:0004834: tryptophan synthase activity molecular_function |
| Author | Loftus BJ |
| Entry Date | Apr 20 1999 2:10PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. |
| References | DR ECOCYC; EG11024; trpA
DR PFAM; PF00290; trp_syntA
DR PROSITE; PDOC00151; Tryptophan synthase alpha chain signature
SE TIGR
GA hmmls
AL clustalw, belvu
DR HAMAP; MF_00131; 381 of 384 |
| Genome Property | GenProp0037: tryptophan biosynthesis from ribose-5-phosphate (HMM) |
