A0A7C9PUW8 · A0A7C9PUW8_9CYAN
- ProteinNAD(P)H-quinone oxidoreductase subunit I
- GenendhI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids194 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic activity
- a plastoquinone + NADH + (n+1) H+(in) = a plastoquinol + NAD+ + n H+(out)
a plastoquinone RHEA-COMP:9562 + CHEBI:57945 + (n+1) H+ (in)CHEBI:15378= a plastoquinol RHEA-COMP:9561 + CHEBI:57540 + n H+ (out)CHEBI:15378 - a plastoquinone + NADPH + (n+1) H+(in) = a plastoquinol + NADP+ + n H+(out)
Cofactor
Note: Binds 2 [4Fe-4S] clusters per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 67 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 70 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 74 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 104 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 107 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 110 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 114 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane-derived thylakoid membrane | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | iron ion binding | |
Molecular Function | NADH dehydrogenase (ubiquinone) activity | |
Molecular Function | quinone binding | |
Biological Process | photosynthesis, light reaction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD(P)H-quinone oxidoreductase subunit I
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Oscillatoriales > Oscillatoriaceae > Oscillatoria
Accessions
- Primary accessionA0A7C9PUW8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cellular thylakoid membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
NDH-1 is composed of at least 11 different subunits.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-84 | 4Fe-4S ferredoxin-type | ||||
Sequence: GRIHFEFDKCISCEVCVRVCPINLPVVDWE | ||||||
Domain | 95-124 | 4Fe-4S ferredoxin-type | ||||
Sequence: KHYSIDFGVCIFCANCVEYCPTNCLSATEE | ||||||
Region | 174-194 | Disordered | ||||
Sequence: LPEGALRSGKRPEEIIEESQK | ||||||
Compositional bias | 176-194 | Basic and acidic residues | ||||
Sequence: EGALRSGKRPEEIIEESQK |
Sequence similarities
Belongs to the complex I 23 kDa subunit family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length194
- Mass (Da)22,524
- Last updated2021-02-10 v1
- ChecksumDD52A2D94D777E08
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 176-194 | Basic and acidic residues | ||||
Sequence: EGALRSGKRPEEIIEESQK |