yegQ protein (Aeromonas schubertii) - STRING interaction network

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Score

yegQ

Protease. (454 aa)

Predicted Functional Partners:

yfhL

0.888

nuoC

0.887

yhbV

0.780

ALP39978.1

0.750

yhbT

0.677

ALP40946.1

0.603

hemN

0.499

ALP42720.1

0.470

pmp3

0.470

ALP40390.1

0.437

Your Current Organism:

Aeromonas schubertii

NCBI taxonomy Id: 652
Other names: A. schubertii, ATCC 43700, Aeromonas hybridization group 12, CCUG 27820, CDC 2446-81, CECT 4240, CIP 103437, DSM 4882, Enteric Group 501, JCM 7373, LMG 9074, LMG:9074

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ALP39978.1	nuoC	WL1483_559	WL1483_2074	Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	NADH: ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.	0.999
ALP39978.1	yegQ	WL1483_559	WL1483_960	Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Protease.	0.750
ALP39978.1	yfhL	WL1483_559	WL1483_517	Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Ferredoxin.	0.934
ALP39978.1	yhbV	WL1483_559	WL1483_3406	Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	Protease.	0.750
ALP40390.1	yegQ	WL1483_971	WL1483_960	Hypothetical protein.	Protease.	0.437
ALP40390.1	yfhL	WL1483_971	WL1483_517	Hypothetical protein.	Ferredoxin.	0.437
ALP40946.1	yegQ	WL1483_1527	WL1483_960	O-methyltransferase.	Protease.	0.603
ALP40946.1	yhbV	WL1483_1527	WL1483_3406	O-methyltransferase.	Protease.	0.603
ALP42720.1	pmp3	WL1483_3301	WL1483_4773	Acetyltransferase.	Membrane protein.	0.773
ALP42720.1	yegQ	WL1483_3301	WL1483_960	Acetyltransferase.	Protease.	0.470
ALP42720.1	yfhL	WL1483_3301	WL1483_517	Acetyltransferase.	Ferredoxin.	0.470
hemN	yegQ	WL1483_1623	WL1483_960	Coproporphyrinogen III oxidase; Belongs to the anaerobic coproporphyrinogen-III oxidase family.	Protease.	0.499
nuoC	ALP39978.1	WL1483_2074	WL1483_559	NADH: ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.	Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.999
nuoC	yegQ	WL1483_2074	WL1483_960	NADH: ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.	Protease.	0.887
nuoC	yfhL	WL1483_2074	WL1483_517	NADH: ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.	Ferredoxin.	0.999
nuoC	yhbV	WL1483_2074	WL1483_3406	NADH: ubiquinone oxidoreductase; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.	Protease.	0.887
pmp3	ALP42720.1	WL1483_4773	WL1483_3301	Membrane protein.	Acetyltransferase.	0.773
pmp3	yegQ	WL1483_4773	WL1483_960	Membrane protein.	Protease.	0.470
pmp3	yfhL	WL1483_4773	WL1483_517	Membrane protein.	Ferredoxin.	0.794
yegQ	ALP39978.1	WL1483_960	WL1483_559	Protease.	Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).	0.750

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