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Information on EC 1.3.1.33 - protochlorophyllide reductase and Organism(s) Prochlorococcus marinus and UniProt Accession Q7VD39

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IUBMB Comments
The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
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This record set is specific for:
Prochlorococcus marinus
UNIPROT: Q7VD39
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Word Map
The taxonomic range for the selected organisms is: Prochlorococcus marinus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
protochlorophyllide oxidoreductase, protochlorophyllide reductase, nadph:protochlorophyllide oxidoreductase, nadph-protochlorophyllide oxidoreductase, por a, por b, dark-operative protochlorophyllide oxidoreductase, osporb, lipor, nadph protochlorophyllide oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dark-operative protochlorophyllide oxidoreductase
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LPOR
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-
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NADPH-protochlorophyllide oxidoreductase
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-
-
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NADPH-protochlorophyllide reductase
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-
-
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NADPH2-protochlorophyllide oxidoreductase
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-
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protochlorophyllide oxidoreductase
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-
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protochlorophyllide photooxidoreductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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SYSTEMATIC NAME
IUBMB Comments
chlorophyllide-a:NADP+ 7,8-oxidoreductase
The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
CAS REGISTRY NUMBER
COMMENTARY hide
68518-04-7
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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
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
heterooctameric complex: subunits N and B are structurally homologous, generating a pseudo-2fold symmetry axis that is colinear with the molecular twofold axis of L2. Both [4Fe-4S] clusters are centered around this extended axis: the L2 cluster is symmetrically ligated by four cysteinyl ligands between the two subunits, whereas the NB cluster is asymmetrically ligated by three cysteine residues from N and one aspartate residue from B
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the X-ray crystallographic structure of the substrate-bound, ADP-aluminium fluoride-stabilized (ADP-AlF3-stabilized) transition state complex between the DPOR components L2 and (NB)2 from the marine cyanobacterium Prochlorococcus marinus is reported
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H394A
mutant retains only a moderate activity which points to a critical role of this residue in the specific protonation at C-18, probably by positioning a water molecule at a distance of 3.2 A from C-18 above the ring
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Masuda, T.; Takamiya, K.i.
Novel insights into the enzymology, regulation and physiological functions of light-dependent protochlorophyllide oxidoreductase in angiosperms
Photosynth. Res.
81
1-29
2004
Amaranthus tricolor, Anabaena sp., Arabidopsis thaliana (O48741), Arabidopsis thaliana (P21218), Arabidopsis thaliana (Q42536), Avena sativa (P15904), Bigelowiella natans, Chlamydomonas reinhardtii (Q39617), Cucumis sativus (Q41249), Daucus carota (Q9SDT1), Gloeobacter violaceus, Hordeum vulgare (P13653), Hordeum vulgare (Q42850), Lactuca sativa, Leptolyngbya boryana, Marchantia paleacea (O80333), Nicotiana tabacum (Q8LSZ2), Nicotiana tabacum (Q8LSZ3), Oryza sativa, Pinus mugo, Pinus mugo (Q41203), Pinus strobus, Pinus taeda, Pisum sativum, Prochlorococcus marinus, Solanum lycopersicum, Synechocystis sp. (Q59987), Thermosynechococcus vestitus BP-1, Triticum aestivum (Q41578), Vigna radiata (Q9LKH8)
Manually annotated by BRENDA team
Moser, J.; Lange, C.; Krausze, J.; Rebelein, J.; Schubert, W.D.; Ribbe, M.W.; Heinz, D.W.; Jahn, D.
Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex
Proc. Natl. Acad. Sci. USA
110
2094-2098
2013
Prochlorococcus marinus (Q7VD39), Prochlorococcus marinus
Manually annotated by BRENDA team