P21883
Gene name |
pdhC (aceC, BSU14600) |
Protein name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex |
Names |
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, E2, S complex, 48 kDa subunit |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU14600 |
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 P21883
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P21883-F1 | Predicted | AlphaFoldDB |
No variants for P21883
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P21883 | |||||
No associated diseases with P21883
4 regional properties for P21883
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Biotin/lipoyl attachment | 1 - 76 | IPR000089 |
| domain | 2-oxoacid dehydrogenase acyltransferase, catalytic domain | 211 - 438 | IPR001078 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 26 - 55 | IPR003016 |
| domain | Peripheral subunit-binding domain | 131 - 169 | 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 |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| dihydrolipoyllysine-residue acetyltransferase activity | Catalysis of the reaction: acetyl-CoA + dihydrolipoamide = CoA + S-acetyldihydrolipoamide. |
| dihydrolipoyllysine-residue succinyltransferase activity | Catalysis of the reaction: succinyl-CoA + dihydrolipoamide = CoA + S-succinyldihydrolipoamide. |
2 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. |
| tricarboxylic acid cycle | A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAFEFKLPDI | GEGIHEGEIV | KWFVKPNDEV | DEDDVLAEVQ | NDKAVVEIPS | PVKGKVLELK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VEEGTVATVG | QTIITFDAPG | YEDLQFKGSD | ESDDAKTEAQ | VQSTAEAGQD | VAKEEQAQEP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AKATGAGQQD | QAEVDPNKRV | IAMPSVRKYA | REKGVDIRKV | TGSGNNGRVV | KEDIDSFVNG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GAQEAAPQET | AAPQETAAKP | AAAPAPEGEF | PETREKMSGI | RKAIAKAMVN | SKHTAPHVTL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MDEVDVTNLV | AHRKQFKQVA | ADQGIKLTYL | PYVVKALTSA | LKKFPVLNTS | IDDKTDEVIQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KHYFNIGIAA | DTEKGLLVPV | VKNADRKSVF | EISDEINGLA | TKAREGKLAP | AEMKGASCTI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TNIGSAGGQW | FTPVINHPEV | AILGIGRIAE | KAIVRDGEIV | AAPVLALSLS | FDHRMIDGAT |
| 430 | 440 | ||||
| AQNALNHIKR | LLNDPQLILM | EA |