phaD protein (Polyangium brachysporum) - STRING interaction network

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Score

phaD

Monovalent cation/H+ antiporter subunit D. (569 aa)

Predicted Functional Partners:

phaE

0.999

phaC

0.999

phaA

0.999

phaG

0.998

phaF

0.998

nuoL

0.967

nuoI

0.814

AAW51_1039

0.811

nuoB

0.757

nuoC

0.699

Your Current Organism:

Polyangium brachysporum

NCBI taxonomy Id: 413882
Other names: ATCC 53080, DSM 7029, NBRC 100090, [. brachysporum, [Polyangium] brachysporum, strain K481-B101

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AAW51_1039	nuoB	AAW51_1039	AAW51_1737	Ferredoxin.	NADH dehydrogenase; 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.	0.985
AAW51_1039	nuoC	AAW51_1039	AAW51_1738	Ferredoxin.	NADH dehydrogenase; 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; Belongs to the complex I 30 kDa subunit family.	0.985
AAW51_1039	nuoL	AAW51_1039	AAW51_1747	Ferredoxin.	NADH:ubiquinone oxidoreductase subunit L.	0.960
AAW51_1039	phaA	AAW51_1039	AAW51_3381	Ferredoxin.	Monovalent cation/H+ antiporter subunit A.	0.997
AAW51_1039	phaC	AAW51_1039	AAW51_3380	Ferredoxin.	Monovalent cation/H+ antiporter subunit C.	0.692
AAW51_1039	phaD	AAW51_1039	AAW51_3379	Ferredoxin.	Monovalent cation/H+ antiporter subunit D.	0.811
AAW51_1039	phaE	AAW51_1039	AAW51_3378	Ferredoxin.	Monovalent cation/H+ antiporter subunit E.	0.528
AAW51_1039	phaF	AAW51_1039	AAW51_3377	Ferredoxin.	Cation:proton antiporter.	0.414
AAW51_1039	phaG	AAW51_1039	AAW51_3376	Ferredoxin.	Cation:proton antiporter.	0.414
nuoB	AAW51_1039	AAW51_1737	AAW51_1039	NADH dehydrogenase; 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.	Ferredoxin.	0.985
nuoB	nuoC	AAW51_1737	AAW51_1738	NADH dehydrogenase; 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.	NADH dehydrogenase; 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; Belongs to the complex I 30 kDa subunit family.	0.999
nuoB	nuoI	AAW51_1737	AAW51_1744	NADH dehydrogenase; 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.	NADH dehydrogenase; 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.	0.998
nuoB	nuoL	AAW51_1737	AAW51_1747	NADH dehydrogenase; 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.	NADH:ubiquinone oxidoreductase subunit L.	0.994
nuoB	phaA	AAW51_1737	AAW51_3381	NADH dehydrogenase; 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.	Monovalent cation/H+ antiporter subunit A.	0.993
nuoB	phaC	AAW51_1737	AAW51_3380	NADH dehydrogenase; 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.	Monovalent cation/H+ antiporter subunit C.	0.662
nuoB	phaD	AAW51_1737	AAW51_3379	NADH dehydrogenase; 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.	Monovalent cation/H+ antiporter subunit D.	0.757
nuoB	phaE	AAW51_1737	AAW51_3378	NADH dehydrogenase; 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.	Monovalent cation/H+ antiporter subunit E.	0.662
nuoB	phaF	AAW51_1737	AAW51_3377	NADH dehydrogenase; 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.	Cation:proton antiporter.	0.662
nuoB	phaG	AAW51_1737	AAW51_3376	NADH dehydrogenase; 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.	Cation:proton antiporter.	0.662
nuoC	AAW51_1039	AAW51_1738	AAW51_1039	NADH dehydrogenase; 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; Belongs to the complex I 30 kDa subunit family.	Ferredoxin.	0.985