node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
bchB | bchC | RPA1543 | RPA1521 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.792 |
bchB | bchF | RPA1543 | RPA1541 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Possible 2-vinyl bacteriochlorophillide hydratase BchF subunit (AB034704). | 0.997 |
bchB | bchG | RPA1543 | RPA1530 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Geranylgeranyl bacteriochlorophyll synthase. | 0.982 |
bchB | bchL | RPA1543 | RPA1545 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Protochlorophyllide reductase iron-sulfur ATP-binding protein BchL; 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. | 0.999 |
bchB | bchN | RPA1543 | RPA1542 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Protochlorophyllide reductase subunit BchN; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | 0.999 |
bchB | bchX | RPA1543 | RPA1522 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Bacteriochlorophyllide reductase subunit BchX; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the NifH/BchL/ChlL family. | 0.986 |
bchB | bchY | RPA1543 | RPA1523 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Bacteriochlorophyllide reductase subunit BchY; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.988 |
bchB | bchZ | RPA1543 | RPA1524 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Bacteriochlorophyllide reductase subunit; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.945 |
bchB | pufL | RPA1543 | RPA1527 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Photosynthetic reaction center L subunit; The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | 0.790 |
bchB | pufM | RPA1543 | RPA1528 | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | Photosynthetic reaction center M protein; The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | 0.791 |
bchC | bchB | RPA1521 | RPA1543 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Protochlorophyllide reductase BchB subunit; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | 0.792 |
bchC | bchF | RPA1521 | RPA1541 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible 2-vinyl bacteriochlorophillide hydratase BchF subunit (AB034704). | 0.995 |
bchC | bchG | RPA1521 | RPA1530 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Geranylgeranyl bacteriochlorophyll synthase. | 0.983 |
bchC | bchL | RPA1521 | RPA1545 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Protochlorophyllide reductase iron-sulfur ATP-binding protein BchL; 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. | 0.772 |
bchC | bchN | RPA1521 | RPA1542 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Protochlorophyllide reductase subunit BchN; 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 NB-protein (BchN-BchB) is the catalytic component of the complex. | 0.834 |
bchC | bchX | RPA1521 | RPA1522 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Bacteriochlorophyllide reductase subunit BchX; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the NifH/BchL/ChlL family. | 0.999 |
bchC | bchY | RPA1521 | RPA1523 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Bacteriochlorophyllide reductase subunit BchY; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.998 |
bchC | bchZ | RPA1521 | RPA1524 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Bacteriochlorophyllide reductase subunit; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.998 |
bchC | pufL | RPA1521 | RPA1527 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Photosynthetic reaction center L subunit; The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | 0.804 |
bchC | pufM | RPA1521 | RPA1528 | 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Photosynthetic reaction center M protein; The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | 0.812 |