Q9D051
Gene name |
Pdhb |
Protein name |
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial |
Names |
PDHE1-B |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:68263 |
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 Q9D051
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9D051-F1 | Predicted | AlphaFoldDB |
15 variants for Q9D051
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs224674946 | 5 | A>T | No | EVA | |
| rs3389291695 | 74 | W>* | No | EVA | |
| rs3389233878 | 75 | K>R | No | EVA | |
| rs3389233946 | 77 | Y>* | No | EVA | |
| rs3389310007 | 77 | Y>D | No | EVA | |
| rs3389280856 | 83 | I>V | No | EVA | |
| rs3389322773 | 89 | E>D | No | EVA | |
| rs3404151604 | 107 | I>* | No | EVA | |
| rs3405154383 | 111 | M>I | No | EVA | |
| rs3389305740 | 178 | W>R | No | EVA | |
| rs3389310269 | 256 | L>V | No | EVA | |
| rs3389314403 | 276 | I>N | No | EVA | |
| rs3389291687 | 302 | G>S | No | EVA | |
| rs3389322834 | 304 | E>G | No | EVA | |
| rs3389310211 | 320 | A>G | No | EVA |
No associated diseases with Q9D051
No regional properties for Q9D051
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9D051 | |||
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 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. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| 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. |
4 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. |
| 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. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P11966 | PDHB | Pyruvate dehydrogenase E1 component subunit beta, mitochondrial | Bos taurus (Bovine) | PR |
| P11177 | PDHB | Pyruvate dehydrogenase E1 component subunit beta, mitochondrial | Homo sapiens (Human) | PR |
| P49432 | Pdhb | Pyruvate dehydrogenase E1 component subunit beta, mitochondrial | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAVVAGLVRG | PLRQASGLLK | RRFHRSAPAA | VQLTVREAIN | QGMDEELERD | EKVFLLGEEV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AQYDGAYKVS | RGLWKKYGDK | RIIDTPISEM | GFAGIAVGAA | MAGLRPICEF | MTFNFSMQAI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DQVINSAAKT | YYMSAGLQPV | PIVFRGPNGA | SAGVAAQHSQ | CFAAWYGHCP | GLKVVSPWNS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EDAKGLIKSA | IRDNNPVVML | ENELMYGVAF | ELPAEAQSKD | FLIPIGKAKI | ERQGTHITVV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AHSRPVGHCL | EAAAVLSKEG | IECEVINLRT | IRPMDIEAIE | ASVMKTNHLV | TVEGGWPQFG |
| 310 | 320 | 330 | 340 | 350 | |
| VGAEICARIM | EGPAFNFLDA | PAVRVTGADV | PMPYAKVLED | NSVPQVKDII | FAVKKTLNI |