| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| atpF1 | atpF2 | sce9363 | sce9364 | H(+)-transporting two-sector ATPase; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | H(+)-transporting two-sector ATPase; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. | 0.995 |
| atpF1 | sce1623 | sce9363 | sce1623 | H(+)-transporting two-sector ATPase; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Membrane protein, putative; Specificity unclear. | 0.529 |
| atpF1 | sce3782 | sce9363 | sce3782 | H(+)-transporting two-sector ATPase; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Zn-ribbon protein possibly nucleic acid-binding. | 0.663 |
| atpF1 | sce7223 | sce9363 | sce7223 | H(+)-transporting two-sector ATPase; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | Hypothetical protein. | 0.631 |
| atpF2 | atpF1 | sce9364 | sce9363 | H(+)-transporting two-sector ATPase; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. | H(+)-transporting two-sector ATPase; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. | 0.995 |
| atpF2 | sce1623 | sce9364 | sce1623 | H(+)-transporting two-sector ATPase; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. | Membrane protein, putative; Specificity unclear. | 0.543 |
| atpF2 | sce3782 | sce9364 | sce3782 | H(+)-transporting two-sector ATPase; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. | Zn-ribbon protein possibly nucleic acid-binding. | 0.488 |
| hemA | hemC | sce1624 | sce1625 | Glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | 0.999 |
| hemA | sce1622 | sce1624 | sce1622 | Glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Hypothetical protein predicted by Glimmer/Critica. | 0.550 |
| hemA | sce1623 | sce1624 | sce1623 | Glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Membrane protein, putative; Specificity unclear. | 0.883 |
| hemA | sce1626 | sce1624 | sce1626 | Glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Hypothetical protein; Belongs to the glycosyl hydrolase 57 family. | 0.509 |
| hemC | hemA | sce1625 | sce1624 | Hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | Glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | 0.999 |
| hemC | sce1622 | sce1625 | sce1622 | Hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | Hypothetical protein predicted by Glimmer/Critica. | 0.543 |
| hemC | sce1623 | sce1625 | sce1623 | Hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | Membrane protein, putative; Specificity unclear. | 0.813 |
| hemC | sce1626 | sce1625 | sce1626 | Hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | Hypothetical protein; Belongs to the glycosyl hydrolase 57 family. | 0.559 |
| lolA1 | pyrE | sce5076 | sce0446 | Putative exported protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Putative orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | 0.417 |
| lolA1 | sce1623 | sce5076 | sce1623 | Putative exported protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Membrane protein, putative; Specificity unclear. | 0.535 |
| lolA1 | sce3782 | sce5076 | sce3782 | Putative exported protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Zn-ribbon protein possibly nucleic acid-binding. | 0.625 |
| lolA1 | sce7223 | sce5076 | sce7223 | Putative exported protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | Hypothetical protein. | 0.606 |
| pyrE | lolA1 | sce0446 | sce5076 | Putative orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). | Putative exported protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). | 0.417 |