Information on EC 1.17.7.2 - 7-hydroxymethyl chlorophyll a reductase

for references in articles please use BRENDA:EC1.17.7.2
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

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EC NUMBER
COMMENTARY hide
1.17.7.2
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RECOMMENDED NAME
GeneOntology No.
7-hydroxymethyl chlorophyll a reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chlorophyll a + H2O + 2 oxidized ferredoxin = 71-hydroxychlorophyll a + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
chlorophyll cycle
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chlorophyll metabolism
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Porphyrin and chlorophyll metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
71-hydroxychlorophyll a:ferredoxin oxidoreductase
Contains FAD and an iron-sulfur center. This enzyme, which is present in plant chloroplasts, carries out the second step in the conversion of chlorophyll b to chlorophyll a. It similarly reduces chlorophyllide a.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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cyanobacterial 3,8-divinyl chlorophyllide reductase (DVR) has 7-hydroxymethyl chlorophyll a reductase activity. Enzyme participates in the Chl cycle in green plants
physiological function
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HCAR functions in Chl degradation as a component of the SGRCCE-LHCII complex during leaf senescence
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7-hydroxymethyl-chlorophyll a + reduced ferredoxin + H+
chlorophyll a + oxidized ferredoxin + H2O
show the reaction diagram
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ir
7-hydroxymethylchlorophyll a + reduced ferredoxin + H+
chlorophyll a + oxidized ferredoxin + H2O
show the reaction diagram
additional information
?
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HCAR interacts with LHCII in in vivo pull-down assays, and with SGR, NYC1, NOL and RCCR in yeast two-hybrid assays
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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
7-hydroxymethyl-chlorophyll a + reduced ferredoxin + H+
chlorophyll a + oxidized ferredoxin + H2O
show the reaction diagram
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ir
7-hydroxymethylchlorophyll a + reduced ferredoxin + H+
chlorophyll a + oxidized ferredoxin + H2O
show the reaction diagram
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HCAR reduces 7-hydroxymethyl chlorophyll a but not 7-hydroxymethyl pheophytin a or 7-hydroxymethyl pheophorbide a
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?
additional information
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HCAR interacts with LHCII in in vivo pull-down assays, and with SGR, NYC1, NOL and RCCR in yeast two-hybrid assays
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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the enzyme contains FAD
reduced ferredoxin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography
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using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL-21 as a His-tagged fusion protein
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expressed in Escherichia coli BL21 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
HCAR is expressed throughout leaf development and is drastically down-regulated during dark-induced senescence
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HCAR is highly up-regulated during greening of etiolated seedlings
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the enzyme activity is induced upon senescence
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the activity of HMChl reductase is partially down-regulated in mutant hmc1
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LINKS TO OTHER DATABASES (specific for EC-Number 1.17.7.2)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)