| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Bind_1113 | Bind_2337 | Bind_1113 | Bind_2337 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.917 |
| Bind_1113 | Bind_2343 | Bind_1113 | Bind_2343 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | 0.917 |
| Bind_1113 | Bind_2386 | Bind_1113 | Bind_2386 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | KEGG: xau:Xaut_4621 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 0.913 |
| Bind_1113 | Bind_2798 | Bind_1113 | Bind_2798 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | PFAM: peptidase S1 and S6 chymotrypsin/Hap; AAA ATPase central domain protein; SMART: AAA ATPase; KEGG: bra:BRADO4942 hypothetical protein; putative CbxX/CfqX family protein (N-term) and peptidase (C-term). | 0.914 |
| Bind_1113 | Bind_3201 | Bind_1113 | Bind_3201 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | PFAM: TPR repeat-containing protein; Tetratricopeptide TPR_3; Tetratricopeptide TPR_4; Tetratricopeptide TPR_2 repeat protein; SMART: Tetratricopeptide domain protein; KEGG: bur:Bcep18194_B1065 TPR repeat protein. | 0.825 |
| Bind_1113 | nuoB | Bind_1113 | Bind_2398 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | NADH-quinone oxidoreductase, B subunit; 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. | 0.942 |
| Bind_1113 | nuoC | Bind_1113 | Bind_2397 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | NADH (or F420H2) dehydrogenase, subunit C; 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. | 0.954 |
| Bind_1113 | nuoD1 | Bind_1113 | Bind_2396 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | NADH dehydrogenase I, D subunit; 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. | 0.911 |
| Bind_1113 | nuoN | Bind_1113 | Bind_2385 | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | Proton-translocating NADH-quinone oxidoreductase, chain N; 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. | 0.902 |
| Bind_2337 | Bind_1113 | Bind_2337 | Bind_1113 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | 0.917 |
| Bind_2337 | Bind_2386 | Bind_2337 | Bind_2386 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | KEGG: xau:Xaut_4621 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 0.684 |
| Bind_2337 | Bind_2798 | Bind_2337 | Bind_2798 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PFAM: peptidase S1 and S6 chymotrypsin/Hap; AAA ATPase central domain protein; SMART: AAA ATPase; KEGG: bra:BRADO4942 hypothetical protein; putative CbxX/CfqX family protein (N-term) and peptidase (C-term). | 0.626 |
| Bind_2337 | Bind_3201 | Bind_2337 | Bind_3201 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PFAM: TPR repeat-containing protein; Tetratricopeptide TPR_3; Tetratricopeptide TPR_4; Tetratricopeptide TPR_2 repeat protein; SMART: Tetratricopeptide domain protein; KEGG: bur:Bcep18194_B1065 TPR repeat protein. | 0.875 |
| Bind_2337 | nuoB | Bind_2337 | Bind_2398 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | NADH-quinone oxidoreductase, B subunit; 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. | 0.687 |
| Bind_2337 | nuoC | Bind_2337 | Bind_2397 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | NADH (or F420H2) dehydrogenase, subunit C; 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. | 0.665 |
| Bind_2337 | nuoD1 | Bind_2337 | Bind_2396 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | NADH dehydrogenase I, D subunit; 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. | 0.656 |
| Bind_2337 | nuoN | Bind_2337 | Bind_2385 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Proton-translocating NADH-quinone oxidoreductase, chain N; 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. | 0.657 |
| Bind_2343 | Bind_1113 | Bind_2343 | Bind_1113 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | Beta-ketoacyl synthase; PFAM: short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR domain protein; Beta-ketoacyl synthase; Acyl transferase; KEGG: mex:Mext_1947 beta-ketoacyl synthase. | 0.917 |
| Bind_2343 | Bind_2386 | Bind_2343 | Bind_2386 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | KEGG: xau:Xaut_4621 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). | 0.684 |
| Bind_2343 | Bind_2798 | Bind_2343 | Bind_2798 | Peptidyl-prolyl cis-trans isomerase cyclophilin type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. | PFAM: peptidase S1 and S6 chymotrypsin/Hap; AAA ATPase central domain protein; SMART: AAA ATPase; KEGG: bra:BRADO4942 hypothetical protein; putative CbxX/CfqX family protein (N-term) and peptidase (C-term). | 0.626 |