P12695
Gene name |
LAT1 (ODP2, PDA2, YNL071W, N2374) |
Protein name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial |
Names |
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, Pyruvate dehydrogenase complex component E2, PDC-E2, PDCE2 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YNL071W |
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 P12695
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P12695-F1 | Predicted | AlphaFoldDB |
9 variants for P12695
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s14-491680 | 53 | A>S | No | SGRP | |
| s14-491914 | 131 | S>A | No | SGRP | |
| s14-492086 | 188 | G>D | No | SGRP | |
| s14-492085 | 188 | G>S | No | SGRP | |
| s14-492191 | 223 | S>T | No | SGRP | |
| s14-492376 | 285 | I>V | No | SGRP | |
| s14-492423 | 300 | N>K | No | SGRP | |
| s14-492842 | 440 | G>E | No | SGRP | |
| s14-492856 | 445 | N>D | No | SGRP |
No associated diseases with P12695
No regional properties for P12695
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P12695 | |||
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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial pyruvate dehydrogenase complex | Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA in eukaryotes; includes subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The This Eukaryotic form usually contains more subunits than its bacterial counterpart; for example, one known complex contains 30 E1 dimers, 60 E2 monomers, and 6 E3 dimers as well as a few copies of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
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 |
|---|---|
| acetyl-CoA biosynthetic process from pyruvate | The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSAFVRVVPR | ISRSSVLTRS | LRLQLRCYAS | YPEHTIIGMP | ALSPTMTQGN | LAAWTKKEGD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QLSPGEVIAE | IETDKAQMDF | EFQEDGYLAK | ILVPEGTKDI | PVNKPIAVYV | EDKADVPAFK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DFKLEDSGSD | SKTSTKAQPA | EPQAEKKQEA | PAEETKTSAP | EAKKSDVAAP | QGRIFASPLA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KTIALEKGIS | LKDVHGTGPR | GRITKADIES | YLEKSSKQSS | QTSGAAAATP | AAATSSTTAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SAPSPSSTAS | YEDVPISTMR | SIIGERLLQS | TQGIPSYIVS | SKISISKLLK | LRQSLNATAN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DKYKLSINDL | LVKAITVAAK | RVPDANAYWL | PNENVIRKFK | NVDVSVAVAT | PTGLLTPIVK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NCEAKGLSQI | SNEIKELVKR | ARINKLAPEE | FQGGTICISN | MGMNNAVNMF | TSIINPPQST |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ILAIATVERV | AVEDAAAENG | FSFDNQVTIT | GTFDHRTIDG | AKGAEFMKEL | KTVIENPLEM |
| LL |