nuoA protein (Acidovorax avenae) - STRING interaction network

This is the evidence view. Different line colors represent the types of evidence for the association.




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Your Input:
	nuoA	NADH-quinone oxidoreductase subunit A; 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 (By similarity) (119 aa)
		(Acidovorax avenae)
Predicted Functional Partners:
	nuoH	NADH-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron- su [...] (358 aa)	•	•	•	•	•	•	0.999
	nuoB	NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron- su [...] (159 aa)	•	•	•		•	•	0.999
	nuoC	NADH-quinone oxidoreductase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron- su [...] (202 aa)	•	•		•	•	•	0.999
	Aave_1276	Proton-translocating NADH-quinone oxidoreductase, chain N (497 aa)	•	•	•	•	•	•	0.998
	nuoD	NADH-quinone oxidoreductase subunit D; NDH-1 shuttles electrons from NADH, via FMN and iron- su [...] (417 aa)	•	•	•		•	•	0.998
	Aave_1275	Proton-translocating NADH-quinone oxidoreductase, chain M (491 aa)	•	•			•	•	0.997
	Aave_1274	Proton-translocating NADH-quinone oxidoreductase, chain L (678 aa)	•	•			•	•	0.997
	Aave_1273	NADH-ubiquinone oxidoreductase, chain 4L (102 aa)	•	•	•		•	•	0.996
	nuoI	NADH-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron- su [...] (171 aa)	•	•	•		•	•	0.995
	Aave_1267	NADH-quinone oxidoreductase, E subunit (175 aa)	•		•		•	•	0.994

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Info & Parameters ...

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Active Prediction Methods:

Neighborhood Gene Fusion Co-occurrence
Co-expression Experiments Databases Textmining

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