P9WQ75
Gene name |
ilvE (Rv2210c, MTCY190.21c) |
Protein name |
Branched-chain-amino-acid aminotransferase |
Names |
BCAT |
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv2210c |
EC number |
2.6.1.42: Transaminases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
3 structures for P9WQ75
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3HT5 | X-ray | 190 A | A | 1-368 | PDB |
| 5U3F | X-ray | 170 A | A/B | 1-368 | PDB |
| AF-P9WQ75-F1 | Predicted | AlphaFoldDB |
No variants for P9WQ75
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WQ75 | |||||
No associated diseases with P9WQ75
1 regional properties for P9WQ75
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminotransferase, class IV, conserved site | 240 - 273 | IPR018300 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.6.1.42 | Transaminases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| branched-chain-amino-acid transaminase activity | Catalysis of the reaction: a branched-chain amino acid + 2-oxoglutarate = L-glutamate + a 2-oxocarboxylate derived from the branched-chain amino acid. |
| L-isoleucine transaminase activity | Catalysis of the reaction: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoic acid + L-glutamic acid. |
| L-leucine transaminase activity | Catalysis of the reaction: 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamatic acid. |
| L-leucine:2-oxoglutarate aminotransferase activity | Catalysis of the reaction: L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. |
| L-valine transaminase activity | Catalysis of the reaction: 2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoic acid + L-glutamatic acid. |
| pyridoxal phosphate binding | Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| branched-chain amino acid biosynthetic process | The chemical reactions and pathways resulting in the formation of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine. |
| branched-chain amino acid metabolic process | The chemical reactions and pathways involving amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine. |
| isoleucine biosynthetic process | The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid. |
| L-methionine salvage | Any process that generates L-methionine from derivatives of it, without de novo synthesis. |
| leucine biosynthetic process | The chemical reactions and pathways resulting in the formation of leucine, 2-amino-4-methylpentanoic acid. |
| protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine | The modification of peptidyl-lysine to form N6-pyridoxal phosphate-L-lysine. |
| valine biosynthetic process | The chemical reactions and pathways resulting in the formation of valine, 2-amino-3-methylbutanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTSGSLQFTV | LRAVNPATDA | QRESMLREPG | FGKYHTDHMV | SIDYAEGRGW | HNARVIPYGP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IELDPSAIVL | HYAQEVFEGL | KAYRWADGSI | VSFRADANAA | RLRSSARRLA | IPELPDAVFI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ESLRQLIAVD | KAWVPGAGGE | EALYLRPFIF | ATEPGLGVRP | ATQYRYLLIA | SPAGAYFKGG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IAPVSVWVST | EYVRACPGGT | GAAKFGGNYA | ASLLAQAEAA | ENGCDQVVWL | DAVERRYIEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MGGMNIFFVL | GSGGSARLVT | PELSGSLLPG | ITRDSLLQLA | IDAGFAVEER | RIDIDEWQKK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AAAGEITEVF | ACGTAAVITP | VARVRHGASE | FRIADGQPGE | VTMALRDTLT | GIQRGTFADT |
| HGWMARLG |