Q0MQG1 · NDUS1_GORGO
- ProteinNADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- GeneNDUFS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids727 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (By similarity).
Essential for catalysing the entry and efficient transfer of electrons within complex I (By similarity).
Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (By similarity).
Essential for catalysing the entry and efficient transfer of electrons within complex I (By similarity).
Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (By similarity).
Catalytic activity
- a ubiquinone + 5 H+(in) + NADH = a ubiquinol + 4 H+(out) + NAD+
a ubiquinone RHEA-COMP:9565 + 5 H+ (in)CHEBI:15378+ CHEBI:57945 = a ubiquinol RHEA-COMP:9566 + 4 H+ (out)CHEBI:15378+ CHEBI:57540
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [2Fe-2S] cluster per subunit.
Note: Binds 2 [4Fe-4S] clusters per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 75 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 78 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 92 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 124 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 131 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 137 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 176 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 179 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 182 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 226 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | mitochondrion | |
Cellular Component | respiratory chain complex I | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | NADH dehydrogenase (ubiquinone) activity | |
Biological Process | mitochondrial electron transport, NADH to ubiquinone | |
Biological Process | mitochondrial respiratory chain complex I assembly |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Gorilla
Accessions
- Primary accessionQ0MQG1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-23 | Mitochondrion | ||||
Sequence: MLRIPVRKALVGLSKSPKGCVRT | ||||||
Chain | PRO_0000251853 | 24-727 | NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial | |||
Sequence: TATAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEXWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRKNPPKVLFLLGADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDDIEGANYFQQANELSKLVNQQLLADPLVPPQLTIKDFYMTDSISRASQTMAKCVKAVTEGAQAVEEPSIC | ||||||
Modified residue | 84 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 467 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 499 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 709 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Interaction
Subunit
Core subunit of respiratory chain NADH dehydrogenase (Complex I) which is composed of 45 different subunits (By similarity).
This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme (By similarity).
Complex I associates with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (By similarity).
Interacts with MDM2 and AKAP1 (By similarity).
This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme (By similarity).
Complex I associates with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes (By similarity).
Interacts with MDM2 and AKAP1 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-108 | 2Fe-2S ferredoxin-type | ||||
Sequence: NLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEK | ||||||
Domain | 108-147 | 4Fe-4S His(Cys)3-ligated-type | ||||
Sequence: KSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFG | ||||||
Domain | 245-301 | 4Fe-4S Mo/W bis-MGD-type | ||||
Sequence: TRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEXWISDKTRFAYDGLKRQR |
Sequence similarities
Belongs to the complex I 75 kDa subunit family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length727
- Mass (Da)79,450
- Last updated2006-09-19 v1
- Checksum860FE5560CB47D3C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ885673 EMBL· GenBank· DDBJ | ABH12182.1 EMBL· GenBank· DDBJ | mRNA |