P29913 · NQO1_PARDE
- ProteinNADH-quinone oxidoreductase chain 1
- Genenqo1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids431 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic activity
- a quinone + 5 H+(in) + NADH = a quinol + 4 H+(out) + NAD+
CHEBI:132124 + 5 H+ (in)CHEBI:15378+ CHEBI:57945 = CHEBI:24646 + 4 H+ (out)CHEBI:15378+ CHEBI:57540
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FMN.
Note: Binds 1 [4Fe-4S] cluster.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 54-63 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GRGGAGFPTG | ||||||
Binding site | 167-214 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GAGAYICGEETALLESLEGKKGMPRMKPPFPAGAGLYGCPTTVNNVES | ||||||
Binding site | 346 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 349 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 352 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 392 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | respiratory chain complex I | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | FMN binding | |
Molecular Function | metal ion binding | |
Molecular Function | NAD binding | |
Molecular Function | NADH dehydrogenase (ubiquinone) activity | |
Molecular Function | quinone binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameNADH-quinone oxidoreductase chain 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Paracoccus
Accessions
- Primary accessionP29913
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000118566 | 1-431 | NADH-quinone oxidoreductase chain 1 | |||
Sequence: MLNDQDRIFTNLYGMGDRSLAGAKKRGHWDGTAAIIQRGRDKIIDEMKASGLRGRGGAGFPTGMKWSFMPKESDGRPSYLVINADESEPATCKDREIMRHDPHTLIEGALIASFAMGAHAAYIYIRGEFIREREALQAAIDECYDAGLLGRNAAGSGWDFDLYLHHGAGAYICGEETALLESLEGKKGMPRMKPPFPAGAGLYGCPTTVNNVESIAVVPTILRRGAEWFASFGRPNNAGVKLFGLTGHVNTPCVVEEAMSIPMRELIEKHGGGIRGGWKNLKAVIPGGASCPVLTAEQCENAIMDYDGMRDVRSSFGTACMIVMDQSTDVVKAIWRLSKFFKHESCGQCTPCREGTGWMMRVMERLVRGDAEVEEIDMLFDVTKQVEGHTICALGDAAAWPIQGLIRNFREEIEDRIKAKRTGRMGAMAAE |
Keywords
- PTM
Interaction
Subunit
NDH-1 is composed of at least 14 different subunits, Nqo1 to Nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits Nqo7, Nqo8, Nqo10 to Nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers.
Structure
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)47,191
- Last updated1993-04-01 v1
- ChecksumAA25C5A0A7570048
Keywords
- Technical term