A0A1E3RSB5 · A0A1E3RSB5_9MYCO
- ProteinPyruvate dehydrogenase [ubiquinone]
- GenepoxB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids578 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO2. It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone.
Catalytic activity
- a ubiquinone + pyruvate + H2O = a ubiquinol + acetate + CO2
a ubiquinone RHEA-COMP:9565 + CHEBI:15361 + CHEBI:15377 = a ubiquinol RHEA-COMP:9566 + CHEBI:30089 + CHEBI:16526
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 1 thiamine pyrophosphate per subunit.
Activity regulation
The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 49 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 251-254 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TGLL | ||||||
Binding site | 274-278 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TDFPY | ||||||
Binding site | 292 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 408-410 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GSM | ||||||
Binding site | 435 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 435-437 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 462 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 462-468 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: NSSLNFV | ||||||
Site | 467 | Moves into active site upon enzyme activation, plays a role in electron transfer | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | lipid binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | pyruvate dehydrogenase (quinone) activity | |
Molecular Function | thiamine pyrophosphate binding | |
Molecular Function | ubiquinone binding | |
Biological Process | pyruvate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate dehydrogenase [ubiquinone]
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycolicibacterium
Accessions
- Primary accessionA0A1E3RSB5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-115 | Thiamine pyrophosphate enzyme N-terminal TPP-binding | ||||
Sequence: TVAEHLIQALRVSGVRRIYGLPGDSLNGFTDAIRRSGEISWEHVRHEETAAFAAAADAALTGGLAVCAGSCGPGNLHLINGLFDAQRSRVPVLAIAAHIPRTEIGSDYFQETH | ||||||
Region | 183-334 | FAD-binding domain | ||||
Sequence: VVRPDDESLRQAAAILNDARAVTILGGAGVAGAHDALIDLAGTLNAPVVHALRGKEFIEYDNPFDVGMTGLLGFASGYKAIKEADALLMLGTDFPYPQFYPDGAKVIQVDVRGRHLGRRTPVDLGLVGTVADTAAALQPLLQQKTDSQHLDR | ||||||
Domain | 192-319 | Thiamine pyrophosphate enzyme central | ||||
Sequence: RQAAAILNDARAVTILGGAGVAGAHDALIDLAGTLNAPVVHALRGKEFIEYDNPFDVGMTGLLGFASGYKAIKEADALLMLGTDFPYPQFYPDGAKVIQVDVRGRHLGRRTPVDLGLVGTVADTAAAL | ||||||
Domain | 381-527 | Thiamine pyrophosphate enzyme TPP-binding | ||||
Sequence: DVGSPVVWAARYLTMNGRRRLIGSFNHGSMACALPHAIGAQSALPGRQIVALAGDGGLTMLFGELVTLIQNKLPVKVIVFNNSSLNFVELEMKAAGIVNFGTDLVNPDFAAVAQAMGIFGRRVERPADLQRALADAFAHDGPAVVDV | ||||||
Region | 533-574 | Membrane-binding domain | ||||
Sequence: ELSIPPAITVEQAKGFSLYAIRTILAGRADELLDLVTTNVAR |
Domain
Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site.
Sequence similarities
Belongs to the TPP enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length578
- Mass (Da)61,982
- Last updated2017-01-18 v1
- Checksum275289E129319455
Keywords
- Technical term