![]() |
|
Annotation rule MF_00133 |
Accession | MF_00133 |
Dates | 1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 43) |
Name | Trp_synth_beta |
Scope | Bacteria
Archaea |
Templates | P0A2K1 (TRPB_SALTY); P0A879 (TRPB_ECOLI); Q8U093 (TRPB1_PYRFU): [Recover all] |
Triggered by |
Identifier |
|
Protein name |
|
Gene name |
|
Function | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. |
Catalytic activity | RHEA:10532: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
EC 4.2.1.20 |
Cofactor | pyridoxal 5'-phosphate |
Pathway | Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. |
Subunit | Tetramer of two alpha and two beta chains. |
Similarity | Belongs to the TrpB family. |
From: TRPB_ECOLI (P0A879) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
MOD_RES | 87 | 87 | N6-(pyridoxal phosphate)lysine | K |
Size range | 388-459 amino acids |
Related rules | None |
Fusion | None |
Comments | Highly divergent CHLTR; sequence not included in alignment. Duplicated trpB seems of archaebacterial origin. Some archaea have only such form (AERPE), some have only the classical form (METJA) and some have both including two bacteria (AQUAE and THEMA). |