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Literature summary extracted from

  • Zhang, W.; Zhong, H.; Lu, H.; Zhang, Y.; Deng, X.; Huang, K.; Duanmu, D.
    Characterization of ferredoxin-dependent biliverdin reductase PCYA1 reveals the dual function in retrograde bilin biosynthesis and interaction with light-dependent protochlorophyllide oxidoreductase LPOR in Chlamydomonas reinhardtii (2018), Front. Plant Sci., 9, 676 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.3.7.5 additional information Chlamydomonas PCYA1 contains unique N- and C-terminal extensions which exhibit autoactivation activity in yeast two-hybrid system Chlamydomonas reinhardtii

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.33 the coding regions of LPOR (amino acids 35-397) is amplified from pBDCrPCYA1-FDBR vector, cloned into pGADT7 vector, and introduced into Y187 yeast cells, recombinant expression of MBP-tagged enzyme LPOR. Yeast two-hybrid and pull down assay analyses of protein-protein interaction Chlamydomonas reinhardtii

Protein Variants

EC Number Protein Variants Comment Organism
1.3.7.5 additional information identification of mutant pcya1-1, cloning and photosynthetic phenotype analysis, overview. Efficient PCYA1 knockdown by artificial microRNA does not impact algal phototrophic growth. Yeast two-hybrid analyses of protein-protein interaction with bilin biosynthesis metabolism proteins using the coding regions of CrPCYA11TP (amino acids 56-556), CrPCYA1-NTE (amino acids 56-174), CrPCYA1-FDBR (amino acids 175-451), CrPCYA1-CTE (amino acids 449-556), and pull-down assay Chlamydomonas reinhardtii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.33 chloroplast
-
 Chlamydomonas reinhardtii 9507
-
1.3.7.5 chloroplast envelope associated with, PCYA1 is partially associated with chloroplast envelope membrane, consistent with the observed export of bilin from chloroplast to cytosol by cytosolic expression of a bilin-binding reporter protein in Chlamydomonas Chlamydomonas reinhardtii 9941
-
1.3.7.5 thylakoid membrane
-
 Chlamydomonas reinhardtii 42651
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.7.5 Fe2+ in cofactor ferredoxin Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.33 chlorophyllide a + NADP+ Chlamydomonas reinhardtii
-
 protochlorophyllide + NADPH + H+
-
 r
1.3.1.33 chlorophyllide a + NADP+ Chlamydomonas reinhardtii 4A+
-
 protochlorophyllide + NADPH + H+
-
 r
1.3.7.5 biliverdin IXalpha + 4 reduced ferredoxin Chlamydomonas reinhardtii
-
 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
 ?
1.3.7.5 biliverdin IXalpha + 4 reduced ferredoxin Chlamydomonas reinhardtii 4A+
-
 (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.33 Chlamydomonas reinhardtii Q39617
-
-
1.3.1.33 Chlamydomonas reinhardtii 4A+ Q39617
-
-
1.3.7.5 Chlamydomonas reinhardtii A8HUP3
-
-
1.3.7.5 Chlamydomonas reinhardtii 4A+ A8HUP3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.33 chlorophyllide a + NADP+
-
 Chlamydomonas reinhardtii protochlorophyllide + NADPH + H+
-
 r
1.3.1.33 chlorophyllide a + NADP+
-
 Chlamydomonas reinhardtii 4A+ protochlorophyllide + NADPH + H+
-
 r
1.3.7.5 biliverdin IXalpha + 4 reduced ferredoxin
-
 Chlamydomonas reinhardtii (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
 ?
1.3.7.5 biliverdin IXalpha + 4 reduced ferredoxin
-
 Chlamydomonas reinhardtii 4A+ (3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.7.5 More besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively. The extension exhibit auto activation activity Chlamydomonas reinhardtii

Synonyms

EC Number Synonyms Comment Organism
1.3.1.33 Light-dependent protochlorophyllide oxidoreductase
-
 Chlamydomonas reinhardtii
1.3.1.33 LPOR
-
 Chlamydomonas reinhardtii
1.3.1.33 protochlorophyllide reductase
-
 Chlamydomonas reinhardtii
1.3.7.5 FDBR
-
 Chlamydomonas reinhardtii
1.3.7.5 ferredoxin-dependent biliverdin reductase
-
 Chlamydomonas reinhardtii
1.3.7.5 PCYA1
-
 Chlamydomonas reinhardtii
1.3.7.5 phycocyanobilin:ferredoxin oxidoreductase
-
 Chlamydomonas reinhardtii

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.33 NADP+
-
 Chlamydomonas reinhardtii
1.3.1.33 NADPH
-
 Chlamydomonas reinhardtii
1.3.7.5 Ferredoxin
-
 Chlamydomonas reinhardtii

General Information

EC Number General Information Comment Organism
1.3.1.33 metabolism ferredoxin-dependent biliverdin reductase, PCYA1 (EC 1.3.7.5), is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) via its FDBR domain, but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). This interaction is specific to Chlamydomonas since the Arabidopsis thaliana homologous proteins do not interact with each other, yeast two-hybrid and pull down assay analyses of protein-protein interaction Chlamydomonas reinhardtii
1.3.1.33 physiological function light-dependent protochlorophyllide oxidoreductase (LPOR) is a rate-limiting key chlorophyll biosynthetic enzyme Chlamydomonas reinhardtii
1.3.7.5 malfunction both the pcya1-1 mutant with the C-terminal extension of PCYA1 eliminated and efficient knockdown of PCYA1 expression by artificial microRNA exhibit no significant impact on algal phototrophic growth and photosynthetic proteins accumulation, indicating that the conserved FDBR domain is sufficient and minimally required for bilin biosynthesis and functioning. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). The CTE domain of PCYA1 is dispensable for phototrophic growth and photosynthetic proteins accumulation Chlamydomonas reinhardtii
1.3.7.5 metabolism ferredoxin-dependent biliverdin reductase, PCYA1, is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview Chlamydomonas reinhardtii
1.3.7.5 additional information besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively Chlamydomonas reinhardtii
1.3.7.5 physiological function in Chlamydomonas reinhardtii, bilins are not only essential retrograde signals to mitigate oxidative stress during diurnal dark-to-light transitions, they are also required for chlorophyll accumulation and maintenance of a functional photosynthetic apparatus in the light. The ferredoxin-dependent biliverdin reductase, FDBR, is involved in the biosynthesis of bilins. Chlamydomonas phycocyanobilin:ferredoxin oxidoreductase PCYA1 FDBR domain specifically interacts with the rate-limiting chlorophyll biosynthetic enzyme LPOR (light-dependent protochlorophyllide oxidoreductase). CrPCYA1 is a key enzyme involved in bilin biosynthesis in Chlamydomonas. Regulatory role of PCYA1 in chlorophyll biosynthesis via interaction with key Chl biosynthetic enzyme. Chlamydomonas PCYA1 contains unique N- and C-terminal extensions which exhibit autoactivation activity in yeast two-hybrid system Chlamydomonas reinhardtii