Information on EC 1.3.7.15 - chlorophyllide a reductase

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The expected taxonomic range for this enzyme is: Rhodobacter

EC NUMBER
COMMENTARY hide
1.3.7.15
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RECOMMENDED NAME
GeneOntology No.
chlorophyllide a reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
show the reaction diagram
(3)
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33-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
show the reaction diagram
(1)
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bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
show the reaction diagram
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacteriochlorophyll a biosynthesis
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Porphyrin and chlorophyll metabolism
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SYSTEMATIC NAME
IUBMB Comments
bacteriochlorophyllide-a:ferredoxin 7,8-oxidoreductase
The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) [4]. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
show the reaction diagram
additional information
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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
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[4Fe-4S]-center
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is labile in the presence of O2
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of chlorophyllide a reductase with purified proteins. Two Rhodobacter capsulatus strains that overexpress Strep-tagged BchX and BchY are isolated. Strep-tagged BchX is purified as a single polypeptide, and BchZ is co-purified with Strep-tagged BchY. When BchX and BchY-BchZ components are incubated with chlorophyllide a, ATP, and dithionite under anaerobic conditions, chlorophyllide a is converted to a new pigment
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