Information on EC 1.3.7.3 - phycoerythrobilin:ferredoxin oxidoreductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.7.3
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RECOMMENDED NAME
GeneOntology No.
phycoerythrobilin:ferredoxin oxidoreductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phycoerythrobilin biosynthesis I
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phycourobilin biosynthesis
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Porphyrin and chlorophyll metabolism
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SYSTEMATIC NAME
IUBMB Comments
(3Z)-phycoerythrobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha to phycoerythrobilin.
CAS REGISTRY NUMBER
COMMENTARY hide
347401-21-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Fd33
SwissProt
Manually annotated by BRENDA team
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Uniprot
Manually annotated by BRENDA team
strain SS120, strain MED4
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-
Manually annotated by BRENDA team
strain W8020
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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
15,16-dihydrobiliverdin + reduced ferredoxin
show the reaction diagram
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + 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
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
show the reaction diagram
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
show the reaction diagram
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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NADP+
NADPH
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reaction depends on NADPH regenerating system
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30300
-
SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by two affinity chromatography steps to 90% purity and a third gel filtration step
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed using a tac promoter-driven N-terminal GST fusion protein
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gene pebB, recombinant expression of wild-type and mutant enzymes
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into pASK-IBA45+ and transformed in Escherichia coli DH10B cells
into vector pKT270, co-expression with cyanobacterial phytochrome 1 in Escherichia coli JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D107E
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site-directed mutagenesis, the mutant retains activity
D107N
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site-directed mutagenesis, inactive mutant
D231E
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site-directed mutagenesis, the mutant retains activity
D231N
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site-directed mutagenesis, inactive mutant
D107E
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site-directed mutagenesis, the mutant retains activity
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D107N
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site-directed mutagenesis, inactive mutant
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D231E
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site-directed mutagenesis, the mutant retains activity
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D231N
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site-directed mutagenesis, inactive mutant
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (102 entries)
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