1.3.7.4	(3Z)-phytochromobilin + oxidized ferredoxin	-	Avena sativa	biliverdin IXa + reduced ferredoxin	-	287688	
1.3.7.4	(3Z)-phytochromobilin + oxidized ferredoxin	-	Cucumis sativus	biliverdin IXa + reduced ferredoxin	-	287688	
1.3.7.4	(3Z)-phytochromobilin + oxidized ferredoxin	-	Arabidopsis thaliana	biliverdin IXa + reduced ferredoxin	-	287688	
1.3.7.4	(3Z)-phytochromobilin + oxidized ferredoxin	biosynthesis of bilin pigments	Arabidopsis thaliana	biliverdin IXa + reduced ferredoxin	-	287688	
1.3.7.4	(3Z)-phytochromobilin + oxidized ferredoxin	-	Arabidopsis thaliana	biliverdin IXalpha + reduced ferredoxin	-	424401	
1.3.7.4	biliverdin IXalpha + 2 reduced ferredoxin	-	Solanum lycopersicum	(3Z)-phytochromobilin + 2 oxidized ferredoxin	-	460157	
1.3.7.4	biliverdin IXalpha + 2 reduced ferredoxin	-	Cucumis sativus	(3Z)-phytochromobilin + 2 oxidized ferredoxin	-	460157	
1.3.7.4	biliverdin IXalpha + 2 reduced ferredoxin	substrate binding structure analysis, overview	Solanum lycopersicum	(3Z)-phytochromobilin + 2 oxidized ferredoxin	-	460157	
1.3.7.4	biliverdin IXalpha + reduced ferredoxin	-	Zea mays	(3Z)-phytochromobilin + oxidized ferredoxin	-	370880	
1.3.7.4	biliverdin IXalpha + reduced ferredoxin	-	Arabidopsis thaliana	(3Z)-phytochromobilin + oxidized ferredoxin	-	370880	
1.3.7.4	biliverdin IXalpha + reduced ferredoxin	-	Avena sativa	(3Z)-phytochromobilin + oxidized ferredoxin	-	370880	
1.3.7.4	biliverdin IXalpha + reduced ferredoxin	conserved surface-charged residues on HY2 and Arabidopsis ferredoxin AtFd2 are important in the protein-protein interaction as well as biliverdin reduction activity of HY2, mutational analysis, overview. The C12 propionate group of biliverdin is important for HY2-catalyzed biliverdin reduction	Arabidopsis thaliana	(3Z)-phytochromobilin + oxidized ferredoxin	-	370880	
1.3.7.4	additional information	two aspartic acid residues, Asp123 and Asp263, form hydrogen bonds with water molecules and are essential for the site-specific A-ring reduction of biliverdin. PPhiB synthase catalyzes the reduction of BV to produce 2(R), 3Z/E-PPhiB using reducing equivalents from ferredoxin. The 2,3,31,32-diene system of the A-ring is site-specifically reduced. The ZZZssa configurations of BV and PPhiB are displayed as observed in the present crystal structure	Solanum lycopersicum	?	-	89