Information on EC 1.3.7.2 - 15,16-dihydrobiliverdin:ferredoxin oxidoreductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.7.2
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RECOMMENDED NAME
GeneOntology No.
15,16-dihydrobiliverdin:ferredoxin oxidoreductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXalpha + reduced ferredoxin
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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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-
-
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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
15,16-dihydrobiliverdin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of biliverdin IXalpha at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha into phycoerythrobilin.
CAS REGISTRY NUMBER
COMMENTARY hide
347401-20-1
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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
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
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
show the reaction diagram
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
show the reaction diagram
15,16-dihydrobiliverdin + reduced ferredoxin
phycoerythrobilin + oxidized ferredoxin
show the reaction diagram
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
show the reaction diagram
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
phytochromobilin + biliverdin IXa + reduced ferredoxin
phycoerythrobilin
show the reaction diagram
additional information
?
-
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
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
show the reaction diagram
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
show the reaction diagram
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + 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
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechococcus sp. (strain WH8020)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PebA in complex with substrate biliverdin IXalpha, hanging drop vapour diffusion method, 12-20 mg/ml protein in 0.1 M HEPE, pH 7.0, and 28% PEG 4000, 18C, X-ray diffraction structure determination and analysis at 1.55 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by two affinity chromatography steps to 90% purity and a third gel filtration step
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed using a tac promoter-driven N-terminal GST fusion protein
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gene pebA, recombinant expression of wild-type and mutant enzymes, native and selenomethionine-labeled PebA
into pGEX-6P-3 vector for N-terminal fusion with glutathione S-transferase and transformed in Escherichia coli BL21(lambdaDE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D205N
site-directed mutagenesis, the mutant retains activity
D84E
site-directed mutagenesis, the mutant retains activity
D84N
site-directed mutagenesis, inactive mutant
D205N
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site-directed mutagenesis, the mutant retains activity
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D84E
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site-directed mutagenesis, the mutant retains activity
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D84N
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site-directed mutagenesis, inactive mutant
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