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Enzyme Nomenclature
Information on EC 1.3.7.4 - phytochromobilin:ferredoxin oxidoreductase
for references in articles please use BRENDA:EC1.3.7.4
Word Map on EC 1.3.7.4
- 1.3.7.4
-
chromophore
-
phytochrome
-
apophytochrome
- biliverdin
- tetrapyrrole
-
bilins
-
photoreceptors
-
ferredoxin-dependent
-
photoactive
-
holophytochrome
- plastid
- heme
- apoproteins
-
reductases
-
a-ring
-
holoprotein
- ferredoxins
-
light-sensing
- phycoerythrobilin
- pastoris
- ixalpha
- cyanobacteria
- phycocyanobilin
- etioplasts
-
antenna
-
plastid-localized
- biotechnology
- synthesis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.3.7.4
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RECOMMENDED NAME
GeneOntology No.
phytochromobilin:ferredoxin oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3Z)-phytochromobilin + 2 oxidized ferredoxin = biliverdin IXalpha + 2 reduced ferredoxin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(3Z)-phytochromobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of biliverdin IXalpha. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin.
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CAS REGISTRY NUMBER
COMMENTARY
138263-99-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, overview
physiological function
physiological function
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HY2 synthesizes the open chain tetrapyrrole chromophore for light-sensing phytochromes. It catalyzes the double bond reduction of a heme-derived tetrapyrrole intermediate biliverdin IXalpha at the A-ring diene system
physiological function
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plants utilize 3Z-phytochromobilin:ferredoxin oxidoreductase to reduce the diene system of the A ring of biliverdin IXalpha to form PthetaB
physiological function
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Hy2 mutants display a long hypocotyl in white light. Mutant seedlings grown under continuous far-red light display a typical blind phenotype showing very long hypocotyls and closed cotyledons. When grown in short-day regime, wild-type bolts after having produced about 44 leaves whereas the null mutants flower after 18 to 20 leaves
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
-
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
biosynthesis of bilin pigments
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-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
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-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
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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
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-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
-
-
-
-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
Q9SR43
biosynthesis of bilin pigments
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-
?
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
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-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
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one of the six Arabidopsis ferredoxins, AtFd2, is the preferred electron donor for HY2. Activity with ferredoxin AtFd2 mutants D78N, E81Q, E82Q, Y89F, R92Q, and D112N, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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NADPH regenerating system with glucose-6-phosphate and glucose-6-phosphate dehydrogenase stimulates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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sub-micromolar Km for biliverdin IXa
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38100
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calculated from amino acid sequence, precursor protein with putative N-terminal plastid transit peptide
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
development of a system to produce phytochromobilin in Escherichia coli by coexpression of heme oxygenase and phytochromobilin:ferredoxin oxidoreductase in a single operon in conjunction with apophytochrome using two compatible plasmids
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overexpression in Synechococcus sp. strain PCC 7002, from endogenous plasmid pAQ1 under the control of the Synechocystis sp. strain PCC 6803 cpcBA promoter, leads to overproduction of phytochromobilin, the cells show a phenotype only slightly less pigmented and blue-green than the wild-type, the strain producing phycobiliproteins carrying phytochromobilin grow much more slowly at low light intensity. Transformant colonies in which pcyA is inactivated in the HY2 overexpression background does not develop a chlorotic appearance, and segregation of the mutant and wild-type alleles is rapidly achieved
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recombinant functional expression of HT-HY2 in Escherichia coli with production of phytochromobilin, functional co-expression with cyanobacterial heme oxygenase, and the phycocyanin alpha-subunit, CpcA, from Synechocystis sp. PCC 6803 or Synechococcus sp. PCC 7002, and with the phycocyanin alpha-subunit phycocyanobilin lyase, CpcE/CpcF, or the phycoerythrocyanin alpha-subunit phycocyanobilin isomerizing lyase, PecE/PecF, from Noctoc sp. PCC 7120. Production levels of fluorescent pigments and chromophore analysis, overview
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D116N
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mutant still retains the ability of substrate binding, but with only 1.5% relative activity of wild type protein
D146N
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mutant completely loses catalytic activity and also the ability of biliverdin binding
E110Q
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site-directed mutagenesis, the mutant shows 321.7% of wild-type activity
E187Q
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site-directed mutagenesis, the mutant shows 20.3% of wild-type activity
H259Q
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site-directed mutagenesis, the mutant shows 123.4% of wild-type activity
K183Q
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site-directed mutagenesis, the mutant shows 24.6% of wild-type activity
K255Q
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site-directed mutagenesis, the mutant shows 11.7% of wild-type activity
K263Q
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site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
R200Q
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site-directed mutagenesis, the mutant shows 12.5% of wild-type activity
R200Q/R264Q
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site-directed mutagenesis, the mutant shows 11.9% of wild-type activity
R252Q
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mutant loses catalytic activity and the ability of substrate binding
R264Q
-
site-directed mutagenesis, the mutant shows 18.9% of wild-type activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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transposon-based directed tagging strategy using maize Ds element generates a wide diversity of tagged and non-tagged alleles that can be used to generate allelic series or deletion of clustered genes
synthesis
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production of full-length plant phytochrome assembled with phytochromobilin in Pichia pastoris by coexpressing apophytochromes and chromophore biosynthetic genes, heme oxygenase (HY1) and phytochromobilin oxidoreductase (HY2) from Arabidopsis thaliana. Mitochondria localization of the phytochromobilin biosynthetic genes increases the efficiency of holophytochrome biosynthesis
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.7.4)
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