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Literature summary for 1.3.1.75 extracted from

  • Suehiro, H.; Tanaka, R.; Ito, H.
    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 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene AM1_2394, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli Acaryochloris marina
gene synw0963, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli Parasynechococcus marenigrum WH 8102

Protein Variants

Protein Variants Comment Organism
additional information BciA and BciB can be readily exchanged, and BciA can be efficiently transferred to cyanobacteria Parasynechococcus marenigrum WH 8102

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3,8-divinyl chlorophyllide a + NADPH + H+ Acaryochloris marina
-
chlorophyllide a + NADP+
-
?
3,8-divinyl chlorophyllide a + NADPH + H+ Parasynechococcus marenigrum WH 8102
-
chlorophyllide a + NADP+
-
?
3,8-divinyl chlorophyllide a + NADPH + H+ Acaryochloris marina MBIC11017
-
chlorophyllide a + NADP+
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+ Acaryochloris marina
-
protochlorophyllide a + NADP+
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+ Parasynechococcus marenigrum WH 8102
-
protochlorophyllide a + NADP+
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+ Acaryochloris marina MBIC11017
-
protochlorophyllide a + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Acaryochloris marina B0C357
-
-
Acaryochloris marina MBIC11017 B0C357
-
-
Parasynechococcus marenigrum WH 8102 Q7U7L8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,8-divinyl chlorophyllide a + NADPH + H+
-
Acaryochloris marina chlorophyllide a + NADP+
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
-
Parasynechococcus marenigrum WH 8102 chlorophyllide a + NADP+
-
?
3,8-divinyl chlorophyllide a + NADPH + H+
-
Acaryochloris marina MBIC11017 chlorophyllide a + NADP+
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
-
Acaryochloris marina protochlorophyllide a + NADP+
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
-
Parasynechococcus marenigrum WH 8102 protochlorophyllide a + NADP+
-
?
3,8-divinyl protochlorophyllide a + NADPH + H+
-
Acaryochloris marina MBIC11017 protochlorophyllide a + NADP+
-
?

Synonyms

Synonyms Comment Organism
8-vinyl reductase
-
Acaryochloris marina
8-vinyl reductase
-
Parasynechococcus marenigrum WH 8102
AM1_2394
-
Acaryochloris marina
BciA
-
Acaryochloris marina
BciA
-
Parasynechococcus marenigrum WH 8102
nmrA
-
Acaryochloris marina
synw0963
-
Parasynechococcus marenigrum WH 8102

Cofactor

Cofactor Comment Organism Structure
additional information BciA contains no cofactor and its reductant is NADPH Acaryochloris marina
additional information BciA contains no cofactor and its reductant is NADPH Parasynechococcus marenigrum WH 8102
NADPH
-
Acaryochloris marina
NADPH
-
Parasynechococcus marenigrum WH 8102

General Information

General Information Comment Organism
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
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
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
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
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
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