| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PMM0899 | hisZ | PMM0899 | PMM0900 | Possible myo-inositol-1(or 4)-monophosphatase; Alternative locus ID: PMED4_10101; Belongs to the inositol monophosphatase superfamily. | Possible Histidyl-tRNA synthetase; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity). | 0.779 |
| PMM0899 | petF | PMM0899 | PMM0898 | Possible myo-inositol-1(or 4)-monophosphatase; Alternative locus ID: PMED4_10101; Belongs to the inositol monophosphatase superfamily. | Ferredoxin, petF-like protein; Alternative locus ID: PMED4_10091. | 0.832 |
| hisZ | PMM0899 | PMM0900 | PMM0899 | Possible Histidyl-tRNA synthetase; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity). | Possible myo-inositol-1(or 4)-monophosphatase; Alternative locus ID: PMED4_10101; Belongs to the inositol monophosphatase superfamily. | 0.779 |
| hisZ | petF | PMM0900 | PMM0898 | Possible Histidyl-tRNA synthetase; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity). | Ferredoxin, petF-like protein; Alternative locus ID: PMED4_10091. | 0.778 |
| ho1 | pcyA | PMM1594 | PMM0747 | Heme oxygenase; Alternative locus ID: PMED4_18041. | Ferredoxin-dependent biliverdin reductase; Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin; Belongs to the HY2 family. | 0.985 |
| ho1 | pebA | PMM1594 | PMM1593 | Heme oxygenase; Alternative locus ID: PMED4_18041. | Phycoerythrobilin:ferredoxin oxidoreductase; Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge; Belongs to the HY2 family. | 0.995 |
| ho1 | petE | PMM1594 | PMM0581 | Heme oxygenase; Alternative locus ID: PMED4_18041. | Plastocyanin; Alternative locus ID: PMED4_06301. | 0.490 |
| ho1 | petF | PMM1594 | PMM0898 | Heme oxygenase; Alternative locus ID: PMED4_18041. | Ferredoxin, petF-like protein; Alternative locus ID: PMED4_10091. | 0.773 |
| ho1 | petF-2 | PMM1594 | PMM1352 | Heme oxygenase; Alternative locus ID: PMED4_18041. | Ferredoxin; Alternative locus ID: PMED4_15201. | 0.800 |
| ho1 | petF-3 | PMM1594 | PMM1449 | Heme oxygenase; Alternative locus ID: PMED4_18041. | Ferredoxin; Alternative locus ID: PMED4_16581. | 0.775 |
| ndhH | petF | PMM0172 | PMM0898 | Putative NADH dehydrogenase subunit; 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. | Ferredoxin, petF-like protein; Alternative locus ID: PMED4_10091. | 0.714 |
| ndhH | petF-2 | PMM0172 | PMM1352 | Putative NADH dehydrogenase subunit; 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. | Ferredoxin; Alternative locus ID: PMED4_15201. | 0.761 |
| ndhH | petF-3 | PMM0172 | PMM1449 | Putative NADH dehydrogenase subunit; 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. | Ferredoxin; Alternative locus ID: PMED4_16581. | 0.710 |
| ndhH | psaF | PMM0172 | PMM0469 | Putative NADH dehydrogenase subunit; 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. | Photosystem I PsaF protein (subunit III); Alternative locus ID: PMED4_05171. | 0.721 |
| pcyA | ho1 | PMM0747 | PMM1594 | Ferredoxin-dependent biliverdin reductase; Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin; Belongs to the HY2 family. | Heme oxygenase; Alternative locus ID: PMED4_18041. | 0.985 |
| pcyA | pebA | PMM0747 | PMM1593 | Ferredoxin-dependent biliverdin reductase; Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin; Belongs to the HY2 family. | Phycoerythrobilin:ferredoxin oxidoreductase; Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge; Belongs to the HY2 family. | 0.978 |
| pcyA | petE | PMM0747 | PMM0581 | Ferredoxin-dependent biliverdin reductase; Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin; Belongs to the HY2 family. | Plastocyanin; Alternative locus ID: PMED4_06301. | 0.522 |
| pcyA | petF | PMM0747 | PMM0898 | Ferredoxin-dependent biliverdin reductase; Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin; Belongs to the HY2 family. | Ferredoxin, petF-like protein; Alternative locus ID: PMED4_10091. | 0.751 |
| pcyA | petF-2 | PMM0747 | PMM1352 | Ferredoxin-dependent biliverdin reductase; Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin; Belongs to the HY2 family. | Ferredoxin; Alternative locus ID: PMED4_15201. | 0.808 |
| pcyA | petF-3 | PMM0747 | PMM1449 | Ferredoxin-dependent biliverdin reductase; Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin; Belongs to the HY2 family. | Ferredoxin; Alternative locus ID: PMED4_16581. | 0.754 |