azo2776 protein (Azoarcus sp. BH72) - STRING interaction network

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azo2776

Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear. (66 aa)

Predicted Functional Partners:

hoxF

0.878

fdh1B

0.878

nuoG

0.844

coxB

0.829

nuoC

0.817

ilvE2

0.805

nuoD

0.795

azo0495

0.766

nuoJ

0.755

nuoN

0.738

Your Current Organism:

Azoarcus sp. BH72

NCBI taxonomy Id: 62928
Other names: A. sp. BH72

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
azo0495	azo2776	azo0495	azo2776	Putative NADH dehydrogenase; 33%; Specificity unclear.	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	0.766
azo0495	coxB	azo0495	azo3304	Putative NADH dehydrogenase; 33%; Specificity unclear.	Conserved hypothetical 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).	0.869
azo0495	fdh1B	azo0495	azo3039	Putative NADH dehydrogenase; 33%; Specificity unclear.	Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl\|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity.	0.998
azo0495	hoxF	azo0495	azo1412	Putative NADH dehydrogenase; 33%; Specificity unclear.	Probable hydrogen dehydrogenase, alpha subunit. Homology to hoxF of A. eutrophus of 41% (sprot\|HOXF_ALCEU). SUBUNITS ALPHA AND GAMMA OF HOXS CONSTITUTE AN NADH-OXIDOREDUCTASE. InterPro: Respiratory-chain NADH dehydrogenase 51 Kd subunit (IPR001949); Respiratory-chain NADH dehydrogenase 24 Kd subunit (IPR002023) Pfam: Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit no signal peptide no TMHs; High confidence in function and specificity.	0.998
azo0495	nuoC	azo0495	azo1398	Putative NADH dehydrogenase; 33%; Specificity unclear.	Respiratory-chain NADH dehydrogenase, chain C probable; 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.	0.992
azo0495	nuoD	azo0495	azo1399	Putative NADH dehydrogenase; 33%; Specificity unclear.	Putative NADH-ubiquinone oxidoreductase chain 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 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 49 kDa subunit family.	0.980
azo0495	nuoG	azo0495	azo1402	Putative NADH dehydrogenase; 33%; Specificity unclear.	Putative NADH-ubiquinone oxidoreductase chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family.	0.959
azo0495	nuoJ	azo0495	azo1405	Putative NADH dehydrogenase; 33%; Specificity unclear.	NADH-ubiquinone oxidoreductase, chain J probable; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.	0.802
azo0495	nuoN	azo0495	azo1409	Putative NADH dehydrogenase; 33%; Specificity unclear.	NADH-ubiquinone oxidoreductase, chain N probable; 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 subunit 2 family.	0.953
azo2776	azo0495	azo2776	azo0495	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Putative NADH dehydrogenase; 33%; Specificity unclear.	0.766
azo2776	coxB	azo2776	azo3304	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Conserved hypothetical 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).	0.829
azo2776	fdh1B	azo2776	azo3039	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Probable formate dehydrogenase (NADP+), beta subunit Homology to fdh1B of M. extorpuens of 55% (trembl\|Q8KTI8) Pfam: Respiratory-chain NADH dehydrogenase 24 kD subunit; Respiratory-chain NADH dehydrogenase 51 kD subunit. no signal peptide no TMHs; High confidence in function and specificity.	0.878
azo2776	hoxF	azo2776	azo1412	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Probable hydrogen dehydrogenase, alpha subunit. Homology to hoxF of A. eutrophus of 41% (sprot\|HOXF_ALCEU). SUBUNITS ALPHA AND GAMMA OF HOXS CONSTITUTE AN NADH-OXIDOREDUCTASE. InterPro: Respiratory-chain NADH dehydrogenase 51 Kd subunit (IPR001949); Respiratory-chain NADH dehydrogenase 24 Kd subunit (IPR002023) Pfam: Respiratory-chain NADH dehydrogenase 24 Kd subunit; Respiratory-chain NADH dehydrogenase 51 Kd subunit no signal peptide no TMHs; High confidence in function and specificity.	0.878
azo2776	ilvE2	azo2776	azo2775	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Branched-chain-amino-acid transaminase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.	0.805
azo2776	nuoC	azo2776	azo1398	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Respiratory-chain NADH dehydrogenase, chain C probable; 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.	0.817
azo2776	nuoD	azo2776	azo1399	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Putative NADH-ubiquinone oxidoreductase chain 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 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 49 kDa subunit family.	0.795
azo2776	nuoG	azo2776	azo1402	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	Putative NADH-ubiquinone oxidoreductase chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family.	0.844
azo2776	nuoJ	azo2776	azo1405	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	NADH-ubiquinone oxidoreductase, chain J probable; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.	0.755
azo2776	nuoN	azo2776	azo1409	Hypothetical protein, 47% identity to TrEMBL;Q7NW97,TrEMBL;Q7VTV4(56% identity). No domains,repeats, motifs or features present; Function unclear.	NADH-ubiquinone oxidoreductase, chain N probable; 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 subunit 2 family.	0.738
coxB	azo0495	azo3304	azo0495	Conserved hypothetical 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 NADH dehydrogenase; 33%; Specificity unclear.	0.869