O59816
Gene name |
lat1 (SPCC794.07) |
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 |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPCC794.07 |
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 O59816
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O59816-F1 | Predicted | AlphaFoldDB |
No variants for O59816
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O59816 | |||||
No associated diseases with O59816
4 regional properties for O59816
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Biotin/lipoyl attachment | 53 - 129 | IPR000089 |
| domain | 2-oxoacid dehydrogenase acyltransferase, catalytic domain | 254 - 483 | IPR001078 |
| binding_site | 2-oxo acid dehydrogenase, lipoyl-binding site | 78 - 107 | IPR003016 |
| domain | Peripheral subunit-binding domain | 186 - 224 | 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 | |
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 |
| MLSANMLRRM | HHGVAVTRML | LVSNGKVQVK | KSALYPVMAK | LARTYATKNY | PAHTVINMPA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSPTMTTGNI | GAFQKKIGDK | IEPGDVLCEI | ETDKAQIDFE | QQDEGYLAKI | LIETGTKDVP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VGKPLAVTVE | NEGDVAAMAD | FTIEDSSAKE | PSAKSGEEKS | APSSEKQSKE | TSSPSNVSGE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ERGDRVFASP | LARKLAEEKD | LDLSQIRGSG | PNGRIIKVDI | ENFKPVVAPK | PSNEAAAKAT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TPAASAADAA | APGDYEDLPL | SNMRKIIASR | LAESKNMNPH | YYVTVSVNME | KIIRLRAALN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AMADGRYKLS | VNDLVIKATT | AALRQVPEVN | AAWMGDFIRQ | YKNVDISMAV | ATPSGLITPV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IRNTHALGLA | EISTLAKDYG | QRARNNKLKP | EEYQGGTFTI | SNLGMFPVDQ | FTAIINPPQA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| CILAVGTTVD | TVVPDSTSEK | GFKVAPIMKC | TLSSDHRVVD | GAMAARFTTA | LKKILENPLE |
| IML |