| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EKE97463.1 | EKE97762.1 | FDUTEX481_04839 | FDUTEX481_04712 | Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. | Alpha/beta hydrolase fold protein; KEGG: mbb:BCG_2299 1.8e-22 lipM; putative esterase LipM K01175; Psort location: CytoplasmicMembrane, score: 10.00. | 0.949 |
| EKE97463.1 | EKF05140.1 | FDUTEX481_04839 | FDUTEX481_01310 | Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. | RNA-binding protein RbpA; KEGG: pmj:P9211_11941 6.0e-19 rbpD; peptidylprolyl isomerase. | 0.844 |
| EKE97463.1 | ndhC | FDUTEX481_04839 | FDUTEX481_03385 | Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. | NADH dehydrogenase subunit A; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.997 |
| EKE97463.1 | ndhH | FDUTEX481_04839 | FDUTEX481_00312 | Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. | NAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.998 |
| EKE97463.1 | ndhJ | FDUTEX481_04839 | FDUTEX481_03387 | Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. | NADH dehydrogenase, subunit C; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.997 |
| EKE97463.1 | ndhK | FDUTEX481_04839 | FDUTEX481_03386 | Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. | NADH dehydrogenase subunit B; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. | 0.998 |
| EKE97762.1 | EKE97463.1 | FDUTEX481_04712 | FDUTEX481_04839 | Alpha/beta hydrolase fold protein; KEGG: mbb:BCG_2299 1.8e-22 lipM; putative esterase LipM K01175; Psort location: CytoplasmicMembrane, score: 10.00. | Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. | 0.949 |
| EKE97762.1 | EKF05140.1 | FDUTEX481_04712 | FDUTEX481_01310 | Alpha/beta hydrolase fold protein; KEGG: mbb:BCG_2299 1.8e-22 lipM; putative esterase LipM K01175; Psort location: CytoplasmicMembrane, score: 10.00. | RNA-binding protein RbpA; KEGG: pmj:P9211_11941 6.0e-19 rbpD; peptidylprolyl isomerase. | 0.831 |
| EKE97762.1 | ndhC | FDUTEX481_04712 | FDUTEX481_03385 | Alpha/beta hydrolase fold protein; KEGG: mbb:BCG_2299 1.8e-22 lipM; putative esterase LipM K01175; Psort location: CytoplasmicMembrane, score: 10.00. | NADH dehydrogenase subunit A; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.936 |
| EKE97762.1 | ndhH | FDUTEX481_04712 | FDUTEX481_00312 | Alpha/beta hydrolase fold protein; KEGG: mbb:BCG_2299 1.8e-22 lipM; putative esterase LipM K01175; Psort location: CytoplasmicMembrane, score: 10.00. | NAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.924 |
| EKE97762.1 | ndhJ | FDUTEX481_04712 | FDUTEX481_03387 | Alpha/beta hydrolase fold protein; KEGG: mbb:BCG_2299 1.8e-22 lipM; putative esterase LipM K01175; Psort location: CytoplasmicMembrane, score: 10.00. | NADH dehydrogenase, subunit C; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. | 0.933 |
| EKE97762.1 | ndhK | FDUTEX481_04712 | FDUTEX481_03386 | Alpha/beta hydrolase fold protein; KEGG: mbb:BCG_2299 1.8e-22 lipM; putative esterase LipM K01175; Psort location: CytoplasmicMembrane, score: 10.00. | NADH dehydrogenase subunit B; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. | 0.939 |
| EKE97789.1 | EKF01001.1 | FDUTEX481_04739 | FDUTEX481_08370 | Putative beta-lactamase-fold exonuclease; KEGG: dme:Dmel_CG1972 6.4e-13 CG1972 gene product from transcript CG1972-RA; Psort location: Cytoplasmic, score: 8.96. | Hypothetical protein; KEGG: cgt:cgR_1633 0.080 phosphoenolpyruvate carboxylase K01595. | 0.910 |
| EKE97789.1 | EKF03236.1 | FDUTEX481_04739 | FDUTEX481_02693 | Putative beta-lactamase-fold exonuclease; KEGG: dme:Dmel_CG1972 6.4e-13 CG1972 gene product from transcript CG1972-RA; Psort location: Cytoplasmic, score: 8.96. | Putative helicase; KEGG: hsl:OE8016F 8.1e-51 ATP-dependent helicase; Psort location: Cytoplasmic, score: 8.96. | 0.910 |
| EKE97789.1 | EKF05140.1 | FDUTEX481_04739 | FDUTEX481_01310 | Putative beta-lactamase-fold exonuclease; KEGG: dme:Dmel_CG1972 6.4e-13 CG1972 gene product from transcript CG1972-RA; Psort location: Cytoplasmic, score: 8.96. | RNA-binding protein RbpA; KEGG: pmj:P9211_11941 6.0e-19 rbpD; peptidylprolyl isomerase. | 0.841 |
| EKE97789.1 | gpmI | FDUTEX481_04739 | FDUTEX481_06927 | Putative beta-lactamase-fold exonuclease; KEGG: dme:Dmel_CG1972 6.4e-13 CG1972 gene product from transcript CG1972-RA; Psort location: Cytoplasmic, score: 8.96. | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. | 0.956 |
| EKF01001.1 | EKE97789.1 | FDUTEX481_08370 | FDUTEX481_04739 | Hypothetical protein; KEGG: cgt:cgR_1633 0.080 phosphoenolpyruvate carboxylase K01595. | Putative beta-lactamase-fold exonuclease; KEGG: dme:Dmel_CG1972 6.4e-13 CG1972 gene product from transcript CG1972-RA; Psort location: Cytoplasmic, score: 8.96. | 0.910 |
| EKF01001.1 | EKF03236.1 | FDUTEX481_08370 | FDUTEX481_02693 | Hypothetical protein; KEGG: cgt:cgR_1633 0.080 phosphoenolpyruvate carboxylase K01595. | Putative helicase; KEGG: hsl:OE8016F 8.1e-51 ATP-dependent helicase; Psort location: Cytoplasmic, score: 8.96. | 0.936 |
| EKF01001.1 | EKF05140.1 | FDUTEX481_08370 | FDUTEX481_01310 | Hypothetical protein; KEGG: cgt:cgR_1633 0.080 phosphoenolpyruvate carboxylase K01595. | RNA-binding protein RbpA; KEGG: pmj:P9211_11941 6.0e-19 rbpD; peptidylprolyl isomerase. | 0.841 |
| EKF01001.1 | gpmI | FDUTEX481_08370 | FDUTEX481_06927 | Hypothetical protein; KEGG: cgt:cgR_1633 0.080 phosphoenolpyruvate carboxylase K01595. | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. | 0.811 |