Q8K9T8
Gene name |
aceF (BUsg_200) |
Protein name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
Names |
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, E2 |
Species |
Buchnera aphidicola subsp Schizaphis graminum (strain Sg) |
KEGG Pathway |
bas:BUsg_200 |
EC number |
2.3.1.12: Transferring groups other than amino-acyl groups |
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 Q8K9T8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8K9T8-F1 | Predicted | AlphaFoldDB |
No variants for Q8K9T8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8K9T8 | |||||
No associated diseases with Q8K9T8
4 regional properties for Q8K9T8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Biotin/lipoyl attachment | 1 - 69 | IPR000089 |
| domain | 2-oxoacid dehydrogenase acyltransferase, catalytic domain | 178 - 409 | IPR001078 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 19 - 48 | IPR003016 |
| domain | Peripheral subunit-binding domain | 112 - 150 | IPR004167 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.12 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| pyruvate dehydrogenase complex | Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| dihydrolipoyllysine-residue acetyltransferase activity | Catalysis of the reaction: acetyl-CoA + dihydrolipoamide = CoA + S-acetyldihydrolipoamide. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| glycolytic process | The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPDIGLEEVE | VTEILVKIGE | EIKLDQGLIT | VEGDKASMEI | PSPISGIVKD | ITIKIGEKVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TSSIIMIFKV | NNLNSIKNEK | DLNYIKTEKK | LNENFLEEKK | DIKKIVLVHA | TPVVRRLARH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LNVDLKNITP | SGPKNRILKE | DIELYIRNNT | SNKSSFNIEK | NNTTNFHKDL | FNEIPITNIQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QIIGKNLHQN | WVNIPHVTQF | DEVNITLLEE | FRHKYNTEKK | QKNNMCSKIT | ILPFIIKSVA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YGLLEFPIFN | SSLSVNKKTI | FLKKYVNVGI | AVDVQNALFV | PVLKNVDKKN | IANLSSELIF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSKKAHENKL | DASDMKDGCF | TISNLGGIGG | SWFSPIINSP | EVAILGVSKA | LIKPLWNGKE |
| 370 | 380 | 390 | 400 | ||
| FIPSLMLPLS | LSYDHRVING | ADAARFLTFI | GKMLSDIRFL | IM |