P33602 · NUOG_ECOLI
- ProteinNADH-quinone oxidoreductase subunit G
- GenenuoG
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids908 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 [2Fe-2S] cluster per subunit.
Note: Binds 3 [4Fe-4S] clusters per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 34 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 45 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 48 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 67 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 99 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 103 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 106 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 112 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 151 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 154 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 157 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 201 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 228 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 231 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 235 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 263 | [4Fe-4S] cluster 3 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Cellular Component | NADH dehydrogenase complex | |
Cellular Component | plasma membrane | |
Cellular Component | plasma membrane respiratory chain complex I | |
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 | molybdopterin cofactor binding | |
Molecular Function | NADH dehydrogenase (ubiquinone) activity | |
Molecular Function | quinone binding | |
Biological Process | aerobic respiration | |
Biological Process | ATP synthesis coupled electron transport | |
Biological Process | cellular respiration | |
Biological Process | respiratory electron transport chain |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameNADH-quinone oxidoreductase subunit G
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP33602
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000118546 | 2-908 | NADH-quinone oxidoreductase subunit G | |||
Sequence: ATIHVDGKEYEVNGADNLLEACLSLGLDIPYFCWHPALGSVGACRQCAVKQYQNAEDTRGRLVMSCMTPASDGTFISIDDEEAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSFRRYRFTKRTHRNQDLGPFISHEMNRCIACYRCVRYYKDYADGTDLGVYGAHDNVYFGRPEDGTLESEFSGNLVEICPTGVFTDKTHSERYNRKWDMQFAPSICQQCSIGCNISPGERYGELRRIENRYNGTVNHYFLCDRGRFGYGYVNLKDRPRQPVQRRGDDFITLNAEQAMQGAADILRQSKKVIGIGSPRASVESNFALRELVGEENFYTGIAHGEQERLQLALKVLREGGIYTPALREIESYDAVLVLGEDVTQTGARVALAVRQAVKGKAREMAAAQKVADWQIAAILNIGQRAKHPLFVTNVDDTRLDDIAAWTYRAPVEDQARLGFAIAHALDNSAPAVDGIEPELQSKIDVIVQALAGAKKPLIISGTNAGSLEVIQAAANVAKALKGRGADVGITMIARSVNSMGLGIMGGGSLEEALTELETGRADAVVVLENDLHRHASAIRVNAALAKAPLVMVVDHQRTAIMENAHLVLSAASFAESDGTVINNEGRAQRFFQVYDPAYYDSKTVMLESWRWLHSLHSTLLSREVDWTQLDHVIDAVVAKIPELAGIKDAAPDATFRIRGQKLAREPHRYSGRTAMRANISVHEPRQPQDIDTMFTFSMEGNNQPTAHRSQVPFAWAPGWNSPQAWNKFQDEVGGKLRFGDPGVRLFETSENGLDYFTSVPARFQPQDGKWRIAPYYHLFGSDELSQRAPVFQSRMPQPYIKLNPADAAKLGVNAGTRVSFSYDGNTVTLPVEIAEGLTAGQVGLPMGMSGIAPVLAGAHLEDLKEAQQ |
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Composed of 13 different subunits. Subunits NuoCD, E, F, and G constitute the peripheral sector of the complex.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P33602 | nuoC P33599 | 2 | EBI-559737, EBI-552399 | |
BINARY | P33602 | nuoE P0AFD1 | 4 | EBI-559737, EBI-1117136 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-83 | 2Fe-2S ferredoxin-type | ||||
Sequence: ATIHVDGKEYEVNGADNLLEACLSLGLDIPYFCWHPALGSVGACRQCAVKQYQNAEDTRGRLVMSCMTPASDGTFISIDDEE | ||||||
Domain | 83-122 | 4Fe-4S His(Cys)3-ligated-type | ||||
Sequence: EAKQFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTG | ||||||
Domain | 221-277 | 4Fe-4S Mo/W bis-MGD-type | ||||
Sequence: MQFAPSICQQCSIGCNISPGERYGELRRIENRYNGTVNHYFLCDRGRFGYGYVNLKD |
Sequence similarities
Belongs to the complex I 75 kDa subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length908
- Mass (Da)100,299
- Last updated2007-01-23 v4
- Checksum7B8626E19709D540
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 188 | in Ref. 1; CAA48366 | ||||
Sequence: T → Q | ||||||
Sequence conflict | 210 | in Ref. 1; CAA48366 | ||||
Sequence: T → K | ||||||
Sequence conflict | 390 | in Ref. 1; CAA48366 | ||||
Sequence: Missing | ||||||
Sequence conflict | 648 | in Ref. 1; CAA48366 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X68301 EMBL· GenBank· DDBJ | CAA48366.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
U00096 EMBL· GenBank· DDBJ | AAC75343.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA16111.2 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
L25055 EMBL· GenBank· DDBJ | AAA03538.1 EMBL· GenBank· DDBJ | Unassigned DNA |