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Enzyme Nomenclature
Information on EC 1.3.7.15 - chlorophyllide a reductase
for references in articles please use BRENDA:EC1.3.7.15
Word Map on EC 1.3.7.15
- 1.3.7.15
- rhodobacter
- protochlorophyllide
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nitrogenase-like
- sphaeroides
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dark-operative
- capsulatus
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8-vinyl
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bchls
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monovinyl
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blastochloris
- barley
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wavelength
- viridis
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iron-sulfur
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b-producing
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reductases
- porphyrin
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purple
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bacteriochlorin
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anoxygenic
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etiochloroplasts
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.3.7.15
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RECOMMENDED NAME
GeneOntology No.
chlorophyllide a reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
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+
(3)
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3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
(1)
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-
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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+
(2)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
heterologous expression of subunits bchXYZ in Synechocystis sp. PCC6803 results in decrease in photosynthetic growth. An increase in cytosolic superoxide dismutase level in the recombinant Synechocystis sp. PCC6803 completely reversed the growth cessation, demonstraing that chlorophyllide a reductase generates superoxide in Synechocystis sp. PCC6803
physiological function
the bchA locus contains three genes bchX, Y and Z, which are essential for the reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a. BchX may supply electrons for reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a
physiological function
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the bchA locus contains three genes bchX, Y and Z, which are essential for the reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a. BchX may supply electrons for reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a
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physiological function
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heterologous expression of subunits bchXYZ in Synechocystis sp. PCC6803 results in decrease in photosynthetic growth. An increase in cytosolic superoxide dismutase level in the recombinant Synechocystis sp. PCC6803 completely reversed the growth cessation, demonstraing that chlorophyllide a reductase generates superoxide in Synechocystis sp. PCC6803
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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
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
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-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
protochlorophyllide + reduced dithionite + ATP + H2O + H+
chlorophyllide a + oxidized dithionite + ADP + phosphate
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-
-
-
?
protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
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-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
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-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
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-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
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-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
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the enzyme catalyses trans-reduction of the B-ring of chlorophyllide a. The product has the (7R,8R)-configuration
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?
additional information
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holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
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additional information
?
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holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
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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
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
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-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
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-
-
-
?
protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
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-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
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-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
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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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C35D
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the mutant of subunit BchZ is inactive; the mutant of subunit BchZ shows 60% of wild type activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.7.15)
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