Information on EC 1.3.7.6 - phycoerythrobilin synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.7.6
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RECOMMENDED NAME
GeneOntology No.
phycoerythrobilin synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3Z)-phycoerythrobilin + 2 oxidized ferredoxin = biliverdin IXalpha + 2 reduced ferredoxin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phycoerythrobilin biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
(3Z)-phycoerythrobilin:ferredoxin oxidoreductase (from biliverdin IXalpha)
This enzyme, from a cyanophage infecting oceanic cyanobacteria of the Prochlorococcus genus, uses a four-electron reduction to carry out the reactions catalysed by EC 1.3.7.2 (15,16-dihydrobiliverdin:ferredoxin oxidoreductase) and EC 1.3.7.3 (phycoerythrobilin:ferredoxin oxidoreductase). 15,16-Dihydrobiliverdin is formed as a bound intermediate. Free 15,16-dihydrobiliverdin can also act as a substrate to form phycoerythrobilin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pebAB
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Manually annotated by BRENDA team
gene pebAB
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Manually annotated by BRENDA team
infecting oceanic cyanobacteria of the Prochlorococcus genus
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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a two-step reaction via intermediate 15,16-dihydrobiliverdin, the single steps form the reactions of EC 1.3.7.2 and 1.3.7.3, overview
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3Z)-phycoerythrobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
show the reaction diagram
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15,16-dihydrobiliverdin is formed as a bound intermediate
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?
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
show the reaction diagram
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?
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phycoerythrobilin + 2 oxidized ferredoxin
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
biliverdin IXalpha + 2 reduced ferredoxin
(3Z)-phycoerythrobilin + 2 oxidized ferredoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structures of substrate complex solved at 1.8- and 2.1 A resolution and of the substrate-free form at 1.55 A resolution. The overall folding reveals an alpha/beta/alpha-sandwich with similarity to the structure of phycocyanobilin:ferredoxin oxidoreductase. The substrate-binding site is located between the central beta-sheet and C-terminal alpha-helices. The substrate binding pocket shows a high flexibility. The substrate is either in a planar porphyrin-like conformation or in a helical conformation and is coordinated by a conserved aspartate/asparagine pair from the beta-sheet side. From the alpha-helix side, a conserved highlyflexible aspartate/proline pair is involved in substrate binding and presumably catalysis
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene pebAB, 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. Colonies of Synechococcus sp. strain PCC 7002 transformed with the pebAB overexpression cassette mostly exhibit a reddish-brown phenotype
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gene pebS, production of His-tagged phycocyanin alpha-subunit-(3Z)-phycoerythrobilin using the alternative FDBR, phycoerythrobilin synthase, PebS, overview. Recombinant functional expression of PebS in Escherichia coli, co-expression with phycocyanin alpha-subunit, CpcA, from Synechocystis sp. PCC 6803 or Synechococcus sp. PCC 7002, cyanobacterial heme oxygenase, 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 hide
LITERATURE
D105N
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site-directed mutagenesis, inactive mutant
additional information