A0A7W7D211 · A0A7W7D211_9ACTN
- ProteinNADH-quinone oxidoreductase subunit I
- GenenuoI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- 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 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 + NADH + 5 H+(in) = a quinol + NAD+ + 4 H+(out)
CHEBI:132124 + CHEBI:57945 + 5 H+ (in)CHEBI:15378= CHEBI:24646 + CHEBI:57540 + 4 H+ (out)CHEBI:15378
Cofactor
Note: Binds 2 [4Fe-4S] clusters per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 43 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 46 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 49 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 53 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 91 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 94 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 97 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 101 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
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 I
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Streptosporangiaceae > Sphaerisporangium
Accessions
- Primary accessionA0A7W7D211
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-63 | 4Fe-4S ferredoxin-type | ||||
Sequence: GVIALVEENCTVCMLCARECPDWCIYIDSH | ||||||
Domain | 82-111 | 4Fe-4S ferredoxin-type | ||||
Sequence: DRFAIDFSLCMYCGICIEVCPFDALFWSPE | ||||||
Region | 155-230 | Disordered | ||||
Sequence: AARPAPGRPSPAAPAAPAGRETPQTRDTPARSEATARAAVRAIRPPGALPKKPSPEGPRERAEKEPPEPSGPAEEP | ||||||
Compositional bias | 208-230 | Basic and acidic residues | ||||
Sequence: SPEGPRERAEKEPPEPSGPAEEP |
Sequence similarities
Belongs to the complex I 23 kDa subunit family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length230
- Mass (Da)25,213
- Last updated2021-06-02 v1
- ChecksumE503060E9606A482
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 208-230 | Basic and acidic residues | ||||
Sequence: SPEGPRERAEKEPPEPSGPAEEP |