Q4QSC5 · NQO9_RHOMR
- ProteinNADH-quinone oxidoreductase subunit 9
- Genenqo9
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids230 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 menaquinone. 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
Note: Binds 2 [4Fe-4S] clusters per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 73 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 76 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 79 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 83 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 113 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 116 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 119 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 123 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane respiratory chain complex I | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | iron ion binding | |
Molecular Function | NADH:ubiquinone reductase (non-electrogenic) activity | |
Molecular Function | quinone binding | |
Biological Process | aerobic respiration |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADH-quinone oxidoreductase subunit 9
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Rhodothermota > Rhodothermia > Rhodothermales > Rhodothermaceae > Rhodothermus
Accessions
- Primary accessionQ4QSC5
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_0000245739 | 1-230 | NADH-quinone oxidoreductase subunit 9 | |||
Sequence: MPGKPVNLASPNERKLNFWERLYLPAVVQGLAYTWRKMRSPRYTFQYPDELWYPPDSYRGRPVLVEENGRPRCVACGLCARACPPLAISMQAKEVDDVKEREPAWFEINMLRCIYCGYCEEVCPEEAIVMSKEYDLTFQSRDEAIFGLEKLLVPAERLKDRLEWLDRYKDPQYGQHWEFRKENNLHSLKDRPFLKWLLEEEGMEELKSTHLRPEEPVAAERSWGGVRAEG |
Keywords
- PTM
Interaction
Subunit
NDH-1 is composed of 14 different subunits. Subunits Nqo7-14 constitute the membrane sector of the complex (By similarity).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 60-93 | 4Fe-4S ferredoxin-type 1 | ||||
Sequence: GRPVLVEENGRPRCVACGLCARACPPLAISMQAK | ||||||
Domain | 104-133 | 4Fe-4S ferredoxin-type 2 | ||||
Sequence: AWFEINMLRCIYCGYCEEVCPEEAIVMSKE |
Sequence similarities
Belongs to the complex I 23 kDa subunit family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length230
- Mass (Da)27,120
- Last updated2005-07-19 v1
- ChecksumE951770E49179E57