| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| APH_1111 | APH_1299 | APH_1111 | APH_1299 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | Identified by similarity to SP:P34943; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF04321; match to protein family HMM PF05368; match to protein family HMM PF07993. | 0.553 |
| APH_1111 | cckA | APH_1111 | APH_0582 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | Sensor histidine kinase/response regulator CckA; Name change according to the cited literature. PMID: 16882029. | 0.577 |
| APH_1111 | fabF | APH_1111 | APH_0930 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 3-oxoacyl-(acyl-carrier-protein) synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.890 |
| APH_1111 | gatC | APH_1111 | APH_1113 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | glutamyl-tRNA(Gln) amidotransferase, C subunit; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. | 0.603 |
| APH_1111 | miaB | APH_1111 | APH_0880 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | tRNA-i(6)A37 thiotransferase enzyme MiaB; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.559 |
| APH_1111 | nuoB | APH_1111 | APH_0520 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | NADH dehydrogenase I, 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. | 0.556 |
| APH_1111 | nuoD | APH_1111 | APH_0732 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins 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. | 0.637 |
| APH_1111 | nuoE | APH_1111 | APH_0731 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | NADH dehydrogenase I, E subunit; Identified by similarity to GB:CAA71011.1; match to protein family HMM PF01257; match to protein family HMM TIGR01958. | 0.573 |
| APH_1111 | nuoI | APH_1111 | APH_0801 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | NADH dehydrogenase I, I 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. | 0.665 |
| APH_1111 | prsA | APH_1111 | APH_1112 | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | Ribose-phosphate pyrophosphokinase; Identified by similarity to SP:P08330; match to protein family HMM PF00156; match to protein family HMM TIGR01251. | 0.582 |
| APH_1299 | APH_1111 | APH_1299 | APH_1111 | Identified by similarity to SP:P34943; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF04321; match to protein family HMM PF05368; match to protein family HMM PF07993. | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.553 |
| APH_1299 | nuoB | APH_1299 | APH_0520 | Identified by similarity to SP:P34943; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF04321; match to protein family HMM PF05368; match to protein family HMM PF07993. | NADH dehydrogenase I, 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. | 0.979 |
| APH_1299 | nuoD | APH_1299 | APH_0732 | Identified by similarity to SP:P34943; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF04321; match to protein family HMM PF05368; match to protein family HMM PF07993. | 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. | 0.979 |
| APH_1299 | nuoE | APH_1299 | APH_0731 | Identified by similarity to SP:P34943; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF04321; match to protein family HMM PF05368; match to protein family HMM PF07993. | NADH dehydrogenase I, E subunit; Identified by similarity to GB:CAA71011.1; match to protein family HMM PF01257; match to protein family HMM TIGR01958. | 0.952 |
| APH_1299 | nuoI | APH_1299 | APH_0801 | Identified by similarity to SP:P34943; match to protein family HMM PF01073; match to protein family HMM PF01370; match to protein family HMM PF04321; match to protein family HMM PF05368; match to protein family HMM PF07993. | NADH dehydrogenase I, I 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. | 0.981 |
| cckA | APH_1111 | APH_0582 | APH_1111 | Sensor histidine kinase/response regulator CckA; Name change according to the cited literature. PMID: 16882029. | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.577 |
| cckA | fabF | APH_0582 | APH_0930 | Sensor histidine kinase/response regulator CckA; Name change according to the cited literature. PMID: 16882029. | 3-oxoacyl-(acyl-carrier-protein) synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | 0.637 |
| cckA | prsA | APH_0582 | APH_1112 | Sensor histidine kinase/response regulator CckA; Name change according to the cited literature. PMID: 16882029. | Ribose-phosphate pyrophosphokinase; Identified by similarity to SP:P08330; match to protein family HMM PF00156; match to protein family HMM TIGR01251. | 0.751 |
| fabF | APH_1111 | APH_0930 | APH_1111 | 3-oxoacyl-(acyl-carrier-protein) synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | ATP-binding protein, Mrp/Nbp35 family; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. | 0.890 |
| fabF | cckA | APH_0930 | APH_0582 | 3-oxoacyl-(acyl-carrier-protein) synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. | Sensor histidine kinase/response regulator CckA; Name change according to the cited literature. PMID: 16882029. | 0.637 |