P53607
Gene name |
ilvA (Bmul_0562, BMULJ_02699) |
Protein name |
L-threonine dehydratase biosynthetic IlvA |
Names |
Threonine deaminase |
Species |
Burkholderia multivorans (strain ATCC 17616 / 249) |
KEGG Pathway |
bmu:Bmul_0562 |
EC number |
4.3.1.19: Ammonia-lyases |
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
1 structures for P53607
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P53607-F1 | Predicted | AlphaFoldDB |
No variants for P53607
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P53607 | |||||
No associated diseases with P53607
4 regional properties for P53607
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| binding_site | Serine/threonine dehydratase, pyridoxal-phosphate-binding site | 43 - 56 | IPR000634 |
| domain | Threonine dehydratase, ACT-like domain | 323 - 412 | IPR001721-1 |
| domain | Threonine dehydratase, ACT-like domain | 424 - 506 | IPR001721-2 |
| domain | Tryptophan synthase beta chain-like, PALP domain | 18 - 310 | IPR001926 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.3.1.19 | Ammonia-lyases |
| 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 |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| L-threonine ammonia-lyase activity | Catalysis of the reaction: L-threonine = 2-oxobutanoate + NH3. |
| 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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| isoleucine biosynthetic process | The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid. |
| threonine metabolic process | The chemical reactions and pathways involving threonine (2-amino-3-hydroxybutyric acid), a polar, uncharged, essential amino acid found in peptide linkage in proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASHDYLKKI | LTARVYDVAF | ETELEPARNL | SARLRNPVYL | KREDNQPVFS | FKLRGAYNKM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AHIPADALAR | GVITASAGNH | AQGVAFSAAR | MGVKAVIVVP | VTTPQVKVDA | VRAHGGPGVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIQAGESYSD | AYAHALKVQE | ERGLTFVHPF | DDPYVIAGQG | TIAMEILRQH | QGPIHAIFVP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IGGGGLAAGV | AAYVKAVRPE | IKVIGVQAED | SCAMAQSLQA | GKRVELAEVG | LFADGTAVKL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VGEETFRLCK | EYLDGVVTVD | TDALCAAIKD | VFQDTRSVLE | PSGALAVAGA | KLYAEREGIE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NQTLVAVTSG | ANMNFDRMRF | VAERAEVGEA | REAVFAVTIP | EERGSFKRFC | SLVGDRNVTE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FNYRIADAQS | AHIFVGVQIR | RRGESADIAA | NFESHGFKTA | DLTHDELSKE | HIRYMVGGRS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PLALDERLFR | FEFPERPGAL | MKFLSSMAPD | WNISLFHYRN | QGADYSSILV | GLQVPQADHA |
| 490 | 500 | ||||
| EFERFLAALG | YPYVEESANP | AYRLFLS |