Q5SLR4
Gene name |
TTHA0229 |
Protein name |
2-oxoisovalerate dehydrogenase subunit alpha |
Names |
Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain, BCKDH E1-alpha |
Species |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
KEGG Pathway |
ttj:TTHA0229 |
EC number |
1.2.4.4: With a disulfide as acceptor |
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
5 structures for Q5SLR4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1UM9 | X-ray | 220 A | A/C | 1-367 | PDB |
| 1UMB | X-ray | 210 A | A/C | 1-367 | PDB |
| 1UMC | X-ray | 240 A | A/C | 1-367 | PDB |
| 1UMD | X-ray | 190 A | A/C | 1-367 | PDB |
| AF-Q5SLR4-F1 | Predicted | AlphaFoldDB |
No variants for Q5SLR4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5SLR4 | |||||
No associated diseases with Q5SLR4
1 regional properties for Q5SLR4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dehydrogenase, E1 component | 43 - 339 | IPR001017 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.4.4 | With a disulfide as acceptor |
| 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 |
|---|---|
| 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity | Catalysis of the reaction: 3-methyl-2-oxobutanoate + lipoamide = S-(2-methylpropanoyl)dihydrolipoamide + CO2. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| branched-chain amino acid catabolic process | The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVKETHRFET | FTEEPIRLIG | EEGEWLGDFP | LDLEGEKLRR | LYRDMLAARM | LDERYTILIR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TGKTSFIAPA | AGHEAAQVAI | AHAIRPGFDW | VFPYYRDHGL | ALALGIPLKE | LLGQMLATKA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DPNKGRQMPE | HPGSKALNFF | TVASPIASHV | PPAAGAAISM | KLLRTGQVAV | CTFGDGATSE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GDWYAGINFA | AVQGAPAVFI | AENNFYAISV | DYRHQTHSPT | IADKAHAFGI | PGYLVDGMDV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LASYYVVKEA | VERARRGEGP | SLVELRVYRY | GPHSSADDDS | RYRPKEEVAF | WRKKDPIPRF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RRFLEARGLW | NEEWEEDVRE | EIRAELERGL | KEAEEAGPVP | PEWMFEDVFA | EKPWHLLRQE |
| ALLKEEL |