node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cbbL | ccmK | Synpcc7942_1426 | Synpcc7942_1421 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | 0.911 |
cbbL | ccmL | Synpcc7942_1426 | Synpcc7942_1422 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Carbon dioxide concentrating mechanism protein CcmL; To E.coli and S.typhimurium CchB. | 0.889 |
cbbL | ccmM | Synpcc7942_1426 | Synpcc7942_1423 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | 0.999 |
cbbL | chlL | Synpcc7942_1426 | Synpcc7942_1419 | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.571 |
ccmK | cbbL | Synpcc7942_1421 | Synpcc7942_1426 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.911 |
ccmK | ccmL | Synpcc7942_1421 | Synpcc7942_1422 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Carbon dioxide concentrating mechanism protein CcmL; To E.coli and S.typhimurium CchB. | 0.997 |
ccmK | ccmM | Synpcc7942_1421 | Synpcc7942_1423 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | 0.962 |
ccmK | chlL | Synpcc7942_1421 | Synpcc7942_1419 | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.663 |
ccmL | cbbL | Synpcc7942_1422 | Synpcc7942_1426 | Carbon dioxide concentrating mechanism protein CcmL; To E.coli and S.typhimurium CchB. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.889 |
ccmL | ccmK | Synpcc7942_1422 | Synpcc7942_1421 | Carbon dioxide concentrating mechanism protein CcmL; To E.coli and S.typhimurium CchB. | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | 0.997 |
ccmL | ccmM | Synpcc7942_1422 | Synpcc7942_1423 | Carbon dioxide concentrating mechanism protein CcmL; To E.coli and S.typhimurium CchB. | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | 0.982 |
ccmM | cbbL | Synpcc7942_1423 | Synpcc7942_1426 | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.999 |
ccmM | ccmK | Synpcc7942_1423 | Synpcc7942_1421 | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | 0.962 |
ccmM | ccmL | Synpcc7942_1423 | Synpcc7942_1422 | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | Carbon dioxide concentrating mechanism protein CcmL; To E.coli and S.typhimurium CchB. | 0.982 |
ccmM | chpX | Synpcc7942_1423 | Synpcc7942_0308 | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | CO2 hydration protein. | 0.896 |
chlL | cbbL | Synpcc7942_1419 | Synpcc7942_1426 | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit; RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | 0.571 |
chlL | ccmK | Synpcc7942_1419 | Synpcc7942_1421 | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | Putative carboxysome assembly protein; May be involved in the formation of the carboxysome, a polyhedral inclusion where RuBisCO is sequestered. | 0.663 |
chlL | hemF | Synpcc7942_1419 | Synpcc7942_0674 | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | Coproporphyrinogen oxidase; Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. | 0.768 |
chpX | ccmM | Synpcc7942_0308 | Synpcc7942_1423 | CO2 hydration protein. | Carbonate dehydratase; The presence of two potential DNA-binding regions suggests this protein may be a transcriptional regulator. | 0.896 |
hemF | chlL | Synpcc7942_0674 | Synpcc7942_1419 | Coproporphyrinogen oxidase; Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | 0.768 |