node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
dmsA | moaD | b0894 | b0784 | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. | Molybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. | 0.658 |
dmsA | moaE | b0894 | b0785 | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | 0.681 |
dmsA | mobB | b0894 | b3856 | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. | Molybdopterin-guanine dinucleotide biosynthesis protein B; GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP. | 0.634 |
dmsA | ynfE | b0894 | b1587 | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. | Putative selenate reductase, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.436 |
dmsA | ynfF | b0894 | b1588 | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. | S- and N-oxide reductase, A subunit, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. | 0.706 |
gapA | groL | b1779 | b4143 | Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.871 |
gapA | trxB | b1779 | b0888 | Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.498 |
groL | gapA | b4143 | b1779 | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Glyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. | 0.871 |
groL | trxB | b4143 | b0888 | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.662 |
moaD | dmsA | b0784 | b0894 | Molybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. | 0.658 |
moaD | moaE | b0784 | b0785 | Molybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | 0.999 |
moaD | mobB | b0784 | b3856 | Molybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. | Molybdopterin-guanine dinucleotide biosynthesis protein B; GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP. | 0.832 |
moaD | ynfE | b0784 | b1587 | Molybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. | Putative selenate reductase, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.660 |
moaD | ynfF | b0784 | b1588 | Molybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. | S- and N-oxide reductase, A subunit, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. | 0.660 |
moaE | dmsA | b0785 | b0894 | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. | 0.681 |
moaE | moaD | b0785 | b0784 | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | Molybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. | 0.999 |
moaE | mobB | b0785 | b3856 | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | Molybdopterin-guanine dinucleotide biosynthesis protein B; GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP. | 0.928 |
moaE | trxB | b0785 | b0888 | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | Thioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. | 0.508 |
moaE | ynfE | b0785 | b1587 | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | Putative selenate reductase, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.703 |
moaE | ynfF | b0785 | b1588 | Molybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | S- and N-oxide reductase, A subunit, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. | 0.702 |