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Literature summary extracted from
- Distribution and functional analysis of the two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria (2021), Arch. Microbiol., 203, 3565-3575 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.1.75 | gene AM1_2394, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli | Acaryochloris marina |
| 1.3.1.75 | gene synw0963, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli | Parasynechococcus marenigrum WH 8102 |
| 1.3.7.13 | gene AM1_2849, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli | Acaryochloris marina |
| 1.3.7.13 | gene slr1923, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli | Synechocystis sp. PCC 6803 |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.3.1.75 | additional information | BciA and BciB can be readily exchanged, and BciA can be efficiently transferred to cyanobacteria | Parasynechococcus marenigrum WH 8102 |
| 1.3.7.13 | additional information | construction of a 8V reductase-deficient Synechocystis by disruption of the slr1923 locus with a chloramphenicol resistance cassette. BciA and BciB can be readily exchanged, and BciA can be efficiently transferred to cyanobacteria | Synechocystis sp. PCC 6803 |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.7.13 | Fe2+ | in the [Fe-S] cluster | Synechocystis sp. PCC 6803 |  |
| 1.3.7.13 | Fe2+ | in the [Fe-S] cluster | Acaryochloris marina | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.75 | 3,8-divinyl chlorophyllide a + NADPH + H+ | Acaryochloris marina | - |
chlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl chlorophyllide a + NADPH + H+ | Parasynechococcus marenigrum WH 8102 | - |
chlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl chlorophyllide a + NADPH + H+ | Acaryochloris marina MBIC11017 | - |
chlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl protochlorophyllide a + NADPH + H+ | Acaryochloris marina | - |
protochlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl protochlorophyllide a + NADPH + H+ | Parasynechococcus marenigrum WH 8102 | - |
protochlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl protochlorophyllide a + NADPH + H+ | Acaryochloris marina MBIC11017 | - |
protochlorophyllide a + NADP+ | - |
? | |
| 1.3.7.13 | chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster | Synechocystis sp. PCC 6803 | - |
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ | - |
? | |
| 1.3.7.13 | chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster | Acaryochloris marina | - |
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ | - |
? | |
| 1.3.7.13 | chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster | Acaryochloris marina MBIC11017 | - |
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.1.75 | Acaryochloris marina | B0C357 | - |
- |
| 1.3.1.75 | Acaryochloris marina MBIC11017 | B0C357 | - |
- |
| 1.3.1.75 | Parasynechococcus marenigrum WH 8102 | Q7U7L8 | - |
- |
| 1.3.7.13 | Acaryochloris marina | B0CAB4 | - |
- |
| 1.3.7.13 | Acaryochloris marina MBIC11017 | B0CAB4 | - |
- |
| 1.3.7.13 | Synechocystis sp. PCC 6803 | P74473 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.75 | 3,8-divinyl chlorophyllide a + NADPH + H+ | - |
Acaryochloris marina | chlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl chlorophyllide a + NADPH + H+ | - |
Parasynechococcus marenigrum WH 8102 | chlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl chlorophyllide a + NADPH + H+ | - |
Acaryochloris marina MBIC11017 | chlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl protochlorophyllide a + NADPH + H+ | - |
Acaryochloris marina | protochlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl protochlorophyllide a + NADPH + H+ | - |
Parasynechococcus marenigrum WH 8102 | protochlorophyllide a + NADP+ | - |
? | |
| 1.3.1.75 | 3,8-divinyl protochlorophyllide a + NADPH + H+ | - |
Acaryochloris marina MBIC11017 | protochlorophyllide a + NADP+ | - |
? | |
| 1.3.7.13 | chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster | - |
Synechocystis sp. PCC 6803 | 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ | - |
? | |
| 1.3.7.13 | chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster | - |
Acaryochloris marina | 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ | - |
? | |
| 1.3.7.13 | chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster | - |
Acaryochloris marina MBIC11017 | 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.1.75 | 8-vinyl reductase | - |
Acaryochloris marina |
| 1.3.1.75 | 8-vinyl reductase | - |
Parasynechococcus marenigrum WH 8102 |
| 1.3.1.75 | AM1_2394 | - |
Acaryochloris marina |
| 1.3.1.75 | BciA | - |
Acaryochloris marina |
| 1.3.1.75 | BciA | - |
Parasynechococcus marenigrum WH 8102 |
| 1.3.1.75 | nmrA | - |
Acaryochloris marina |
| 1.3.1.75 | synw0963 | - |
Parasynechococcus marenigrum WH 8102 |
| 1.3.7.13 | 8-vinyl reductase | - |
Synechocystis sp. PCC 6803 |
| 1.3.7.13 | 8-vinyl reductase | - |
Acaryochloris marina |
| 1.3.7.13 | AM1_2849 | - |
Acaryochloris marina |
| 1.3.7.13 | bciB | - |
Synechocystis sp. PCC 6803 |
| 1.3.7.13 | bciB | - |
Acaryochloris marina |
| 1.3.7.13 | frhB | - |
Acaryochloris marina |
| 1.3.7.13 | Slr1923 | - |
Synechocystis sp. PCC 6803 |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.75 | additional information | BciA contains no cofactor and its reductant is NADPH | Acaryochloris marina | |
| 1.3.1.75 | additional information | BciA contains no cofactor and its reductant is NADPH | Parasynechococcus marenigrum WH 8102 | |
| 1.3.1.75 | NADPH | - |
Acaryochloris marina | |
| 1.3.1.75 | NADPH | - |
Parasynechococcus marenigrum WH 8102 | |
| 1.3.7.13 | FAD | - |
Synechocystis sp. PCC 6803 | |
| 1.3.7.13 | FAD | - |
Acaryochloris marina | |
| 1.3.7.13 | Fe-S center | - |
Synechocystis sp. PCC 6803 | |
| 1.3.7.13 | Fe-S center | - |
Acaryochloris marina | |
| 1.3.7.13 | Ferredoxin | - |
Synechocystis sp. PCC 6803 | |
| 1.3.7.13 | Ferredoxin | - |
Acaryochloris marina | |
| 1.3.7.13 | additional information | BciB contains c, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant | Synechocystis sp. PCC 6803 | |
| 1.3.7.13 | additional information | BciB contains c, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant | Acaryochloris marina |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.3.1.75 | evolution | two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments | Acaryochloris marina |
| 1.3.1.75 | evolution | two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments | Parasynechococcus marenigrum WH 8102 |
| 1.3.1.75 | metabolism | during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciA gene encodes the 8V reductase. BciA contains no cofactor and its reductant is NADPH | Acaryochloris marina |
| 1.3.1.75 | metabolism | during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciA gene encodes the 8V reductase. BciA contains no cofactor and its reductant is NADPH | Parasynechococcus marenigrum WH 8102 |
| 1.3.1.75 | physiological function | in the chlorophyll biosynthesis pathway, the 8-vinyl group of the chlorophyll precursor is reduced to an ethyl group by 8-vinyl reductase. Two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria. Analysis of the enzymatic activity of cyanobacterial BciA, as well as the relationship between BciA occurrence and iron availability in cyanobacteria habitats | Acaryochloris marina |
| 1.3.1.75 | physiological function | in the chlorophyll biosynthesis pathway, the 8-vinyl group of the chlorophyll precursor is reduced to an ethyl group by 8-vinyl reductase. Two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria. Analysis of the enzymatic activity of cyanobacterial BciA, as well as the relationship between BciA occurrence and iron availability in cyanobacteria habitats | Parasynechococcus marenigrum WH 8102 |
| 1.3.7.13 | evolution | two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments | Synechocystis sp. PCC 6803 |
| 1.3.7.13 | evolution | two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments | Acaryochloris marina |
| 1.3.7.13 | metabolism | during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciB gene encodes the 8V reductase. BciB contains an [Fe-S] cluster, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant | Acaryochloris marina |
| 1.3.7.13 | metabolism | during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciB gene encodes the 8V reductase. BciB contains an [Fe-S] cluster, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant. BciB of Synechocystis PCC6803, a model cyanobacterium without chlorophyll b, exhibits both 7-hydroxymethyl chlorophyll a reductase and 8V reductase activity. Synechocystis BciB can convert chlorophyll b to chlorophyll a, but in Synechocystis, such activity has no impact on its metabolism, since it does not synthesize chlorophyll b | Synechocystis sp. PCC 6803 |
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