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Information on EC 1.3.7.7 - ferredoxin:protochlorophyllide reductase (ATP-dependent) and Organism(s) Cereibacter sphaeroides and UniProt Accession Q9RFD6

for references in articles please use BRENDA:EC1.3.7.7
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IUBMB Comments
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. 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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Cereibacter sphaeroides
UNIPROT: Q9RFD6
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The taxonomic range for the selected organisms is: Cereibacter sphaeroides
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
light-independent protochlorophyllide reductase, dark protochlorophyllide reductase, light-independent pchlide reductase, dark-operative pchlide oxidoreductase, dark-operative protochlorophyllide reductase, light-independent (dark-operative) pchlide oxidoreductase, protochlorophyllide oxidoreductase complex, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dark-operative protochlorophyllide reductase
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DPOR
the DPOR holoenzyme is comprised of two component proteins, the dimeric protein L and the heterotetrameric NB-protein
light-independent (dark) Pchlide reductase
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light-independent protochlorophyllide reductase
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dark-operative Pchlide oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
show the reaction diagram
reaction mechanism and structure-function relationship, overview
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SYSTEMATIC NAME
IUBMB Comments
ATP-dependent ferredoxin:protochlorophyllide-a 7,8-oxidoreductase
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. 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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
show the reaction diagram
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-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
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-
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the purified, recombinant protein L contains 3.6 mol of Fe/mol of protein L homodimer, consistent with the presence of a [4Fe-4S] cluster
Fe2+
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in [4Fe-4S] clusters
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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cyanobacteria, algae, bryophytes, pteridophytes and gymnosperms use an additional, light-independent enzyme dubbed dark-operative Pchlide oxidoreductase for chlorophyll biosynthesis, besides a light-dependent enzyme, mechanisms of protochlorophyllide a reduction in photosynthetic organisms, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33310
calculated from amino acid sequence
33380
mass spectroscopy
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN–BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
L-protein of DPOR with Mg-ADP bound, microcapillary batch diffusion method, with 20-25% (w/v) PEG 3350 as the precipitating agent, with 200 mM magnesium formate (pH 7.7)
L-protein in the MgADP-bound form, X-ray diffraction structure determination at 1.6 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
zinc-loaded chelating Sepharose column chromatography and Q-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Azotobacter vinelandii strain DJ884
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sarma, R.; Barney, B.M.; Hamilton, T.L.; Jones, A.; Seefeldt, L.C.; Peters, J.W.
Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: a homologue of the nitrogenase Fe protein
Biochemistry
47
13004-13015
2008
Cereibacter sphaeroides (Q9RFD6), Cereibacter sphaeroides
Manually annotated by BRENDA team
Reinbothe, C.; El Bakkouri, M.; Buhr, F.; Muraki, N.; Nomata, J.; Kurisu, G.; Fujita, Y.; Reinbothe, S.
Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction
Trends Plant Sci.
15
614-624
2010
Cereibacter sphaeroides, Chlorobaculum tepidum, Chloroflexus aurantiacus, Heliobacterium mobile, Prochlorococcus marinus, Rhodobacter capsulatus
Manually annotated by BRENDA team