qcrA protein (Actinoplanes sp. SE50110) - STRING interaction network

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Score

qcrA

Putative menaquinol-cytochrome c reductase iron-sulfur subunit; Rieske Fe-S protein. (365 aa)

Predicted Functional Partners:

ctaE

0.999

qcrC

0.999

qcrB

0.999

ACPL_1643

0.989

ctaC

0.988

nuoE

0.983

nuoI

0.980

nuoI-2

0.980

nuoD

0.979

nuoD-2

0.979

Your Current Organism:

Actinoplanes sp. SE50110

NCBI taxonomy Id: 134676
Other names: A. sp. SE50/110, Actinoplanes sp. (strain 50/110), Actinoplanes sp. 50/110, Actinoplanes sp. SE50/110

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ACPL_1643	ctaC	ACPL_1643	ACPL_1642	Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.	Cytochrome c oxidase subunit II; 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).	0.996
ACPL_1643	ctaE	ACPL_1643	ACPL_1648	Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.	Heme/copper-type cytochrome/quinol oxidase, subunit 3.	0.984
ACPL_1643	qcrA	ACPL_1643	ACPL_1650	Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.	Putative menaquinol-cytochrome c reductase iron-sulfur subunit; Rieske Fe-S protein.	0.989
ACPL_1643	qcrB	ACPL_1643	ACPL_1651	Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.	Cytochrome b subunit of the bc complex.	0.995
ACPL_1643	qcrC	ACPL_1643	ACPL_1649	Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.	Cytochrome c, mono- and diheme variants.	0.987
ctaC	ACPL_1643	ACPL_1642	ACPL_1643	Cytochrome c oxidase subunit II; 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).	Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.	0.996
ctaC	ctaE	ACPL_1642	ACPL_1648	Cytochrome c oxidase subunit II; 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).	Heme/copper-type cytochrome/quinol oxidase, subunit 3.	0.999
ctaC	nuoD	ACPL_1642	ACPL_448	Cytochrome c oxidase subunit II; 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 dehydrogenase I subunit D; 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 a menaquinone. 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 49 kDa subunit family.	0.744
ctaC	nuoD-2	ACPL_1642	ACPL_8067	Cytochrome c oxidase subunit II; 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 dehydrogenase I subunit D; 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 a menaquinone. 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 49 kDa subunit family.	0.744
ctaC	nuoE	ACPL_1642	ACPL_449	Cytochrome c oxidase subunit II; 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 24 kD subunit.	0.903
ctaC	nuoI	ACPL_1642	ACPL_453	Cytochrome c oxidase subunit II; 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 dehydrogenase I subunit I; 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.	0.656
ctaC	nuoI-2	ACPL_1642	ACPL_742	Cytochrome c oxidase subunit II; 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 dehydrogenase I subunit I; 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.	0.656
ctaC	qcrA	ACPL_1642	ACPL_1650	Cytochrome c oxidase subunit II; 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).	Putative menaquinol-cytochrome c reductase iron-sulfur subunit; Rieske Fe-S protein.	0.988
ctaC	qcrB	ACPL_1642	ACPL_1651	Cytochrome c oxidase subunit II; 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).	Cytochrome b subunit of the bc complex.	0.999
ctaC	qcrC	ACPL_1642	ACPL_1649	Cytochrome c oxidase subunit II; 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).	Cytochrome c, mono- and diheme variants.	0.986
ctaE	ACPL_1643	ACPL_1648	ACPL_1643	Heme/copper-type cytochrome/quinol oxidase, subunit 3.	Cytochrome-c oxidase; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family.	0.984
ctaE	ctaC	ACPL_1648	ACPL_1642	Heme/copper-type cytochrome/quinol oxidase, subunit 3.	Cytochrome c oxidase subunit II; 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
ctaE	nuoD	ACPL_1648	ACPL_448	Heme/copper-type cytochrome/quinol oxidase, subunit 3.	NADH dehydrogenase I subunit D; 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 a menaquinone. 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 49 kDa subunit family.	0.734
ctaE	nuoD-2	ACPL_1648	ACPL_8067	Heme/copper-type cytochrome/quinol oxidase, subunit 3.	NADH dehydrogenase I subunit D; 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 a menaquinone. 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 49 kDa subunit family.	0.734
ctaE	nuoE	ACPL_1648	ACPL_449	Heme/copper-type cytochrome/quinol oxidase, subunit 3.	NADH:ubiquinone oxidoreductase 24 kD subunit.	0.906