Aspartate 1-decarboxylase - A5U8S6
Model based on:
Entry features
| GENE | Aspartate 1-decarboxylase | |
|---|---|---|
| DESCRIPTION | Aspartate alpha-decarboxylase | |
| ORGANISM | Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) | |
| TAXONOMY | Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;Mycobacterium; Mycobacterium tuberculosis complex. | |
| UNIPROT | A5U8S6 | |
| Template | 2c45 A | |
| RESISTANCE | pyrazinoic acid |
Cross-references
| STRING | 419947.MtubH3_010100009274 |
|---|---|
| REFSEQ | WP_003419523.1; NZ_CP016972.1 |
| PTM | Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha- subunit with a pyruvoyl group at its N-terminus |
| PFAM | PF02261 - Asp_decarbox |
| KEGG | mra:MRA_3640 |
| EMBL | CP000611; ABQ75426.1 |
| EC | 4.1.1.11 |
| Active site | 25 25 Schiff-base intermediate with substrate; 58 58 Proton donor |
Gene Ontology
| Molecular Function | GO ID | Term | Evidence |
|---|---|---|---|
| GO:0004068 | F:aspartate 1-decarboxylase activity | IEA | |
| Biological Process | GO ID | Term | Evidence |
| GO:0006523 | P:alanine biosynthetic process | IEA | |
| GO:0015940 | P:pantothenate biosynthetic process | IEA | |
| GO:0046677 | P:response to antibiotic | IEA | |
| Cellular Component | GO ID | Term | Evidence |
| GO:0005737 | C:cytoplasm | IEA |
Sequence
Multiple sequence alignment
MSA Mutation
| Variant | Position in MSA |
|---|---|
| L136R | 140 |