P35489
Gene name |
pdhC |
Protein name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
Names |
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, E2 |
Species |
Acholeplasma laidlawii |
KEGG Pathway |
|
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 P35489
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P35489-F1 | Predicted | AlphaFoldDB |
No variants for P35489
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P35489 | |||||
No associated diseases with P35489
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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
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 |
| MYEFKFADIG | EGIHEGTVLQ | WNFKVGDKVK | EGETLVIVET | DKVNAELPSP | VDGTIVSLGA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KEGEEIHVGQ | IIVTIDDGTG | TPAAAPAPAQ | VSAPTPAPAA | APQVAAPAAS | GDIYDFKFAD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IGEGIHEGTI | LQWNFKVGDK | VKEGETLVVV | ETDKVNAELP | SPVDGTILKL | GKAEGEVIHV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GETVVLIGQN | GATLEQAQAP | KAEAPVSEPK | KGAGVVGEIE | VSDDIIGGSE | EVHVVATTGK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VLASPVARKL | ASDLGVDIAT | IKGSGEQGRV | MKDDVQNSKA | PAEAQAPVQQ | TQAPAQAAAS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VAPSFAAAGK | PQGDVEVVKI | TRLRKAVSNA | MTRSKSIIPE | TVLMDEINVD | ALVNFRNEAK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLAESKGIKL | TYMAFIAKAV | LIALKEFPMF | NASFNHDTDE | VYIKKFINLG | MAVDTPDGLI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VPNIKNADRL | SVFELASQVR | SLADDTIARK | ISMDQQTGGT | FTITNFGSAG | IAFGTPVINY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PELAILGIGK | IDRKPWVVGN | EIKIAHTLPL | SLAVDHRIID | GADGGRFLMR | VKELLTNPTL |
| LLLS |