P35487
Gene name |
Pdha2 (Pdha-2, Pdhal) |
Protein name |
Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial |
Names |
PDHE1-A type II |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:18598 |
EC number |
1.2.4.1: With a disulfide as acceptor |
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 P35487
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P35487-F1 | Predicted | AlphaFoldDB |
19 variants for P35487
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388666695 | 23 | R>K | No | EVA | |
| rs3388663951 | 58 | T>I | No | EVA | |
| rs3388671358 | 74 | R>G | No | EVA | |
| rs3388668034 | 93 | H>L | No | EVA | |
| rs3388655490 | 115 | V>L | No | EVA | |
| rs3388647960 | 172 | V>L | No | EVA | |
| rs37097623 | 234 | N>K | No | EVA | |
| rs3388664395 | 237 | S>L | No | EVA | |
| rs1132388827 | 239 | A>S | No | EVA | |
| rs1133284564 | 240 | S>I | No | EVA | |
| rs1134573315 | 241 | T>S | No | EVA | |
| rs3388667098 | 266 | A>V | No | EVA | |
| rs3388667940 | 313 | S>C | No | EVA | |
| rs3388655915 | 320 | L>M | No | EVA | |
| rs3388647925 | 325 | I>F | No | EVA | |
| rs3388660354 | 333 | I>N | No | EVA | |
| rs3388662143 | 351 | A>S | No | EVA | |
| rs3388666740 | 353 | F>C | No | EVA | |
| rs3388666722 | 361 | A>T | No | EVA |
No associated diseases with P35487
1 regional properties for P35487
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dehydrogenase, E1 component | 68 - 362 | IPR001017 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.4.1 | With a disulfide as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| 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. |
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| 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). |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| pyruvate dehydrogenase (acetyl-transferring) activity | Catalysis of the reaction: pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2. |
| pyruvate dehydrogenase (NAD+) activity | Catalysis of the reaction: pyruvate + CoA + NAD+ = acetyl-CoA + CO2 + NADH. |
5 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. |
| glucose metabolic process | The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides. |
| mitochondrial acetyl-CoA biosynthetic process from pyruvate | The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate in the mitochondrion. The process begins with the transport of pyruvate from the cytosol to the mitochondrion where it is subsequently decarboxylated to form acetyl-CoA. |
| pyruvate metabolic process | The chemical reactions and pathways involving pyruvate, 2-oxopropanoate. |
| 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. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q06437 | Pdha2 | Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRKMLTAVLS | HVFSGMVQKP | ALRGLLSSLK | FSNDATCDIK | KCDLYRLEEG | PPTSTVLTRA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EALKYYRTMQ | VIRRMELKAD | QLYKQKFIRG | FCHLCDGQEA | CCVGLEAGIN | PTDHVITSYR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AHGFCYTRGL | SVKSILAELT | GRKGGCAKGK | GGSMHMYGKN | FYGGNGIVGA | QVPLGAGVAF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ACKYLKNGQV | CLALYGDGAA | NQGQVFEAYN | MSALWKLPCV | FICENNLYGM | GTSNERSAAS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TDYHKKGFII | PGLRVNGMDI | LCVREATKFA | ADHCRSGKGP | IVMELQTYRY | HGHSMSDPGI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SYRSREEVHN | VRSKSDPIML | LRERIISNNL | SNIEELKEID | ADVKKEVEDA | AQFATTDPEP |
| 370 | 380 | 390 | |||
| AVEDIANYLY | HQDPPFEVRG | AHKWLKYKSH | S |