1.3.1.33: protochlorophyllide reductase This is an abbreviated version! For detailed information about protochlorophyllide reductase, go to the full flat file .
Reaction
chlorophyllide a +
NADP+ =
protochlorophyllide +
NADPH +
H+
Synonyms 3PCR, B9Z40_03660, bchB, bchL, bchN, dark active protochlorophyllide oxidoreductase, dark operative protochlorophyllide oxidoreductase, dark-operative protochlorophyllide oxidoreductase, DPOR, EH32_03160, faded green leaf, Fgl, GEMMAAP_15250, LHPP, light-activated enzyme protochlorophyllide oxidoreductase, light-dependent NADPH-protochlorophyllide oxidoreductase, light-dependent NADPH: protochlorophyllide oxidoreductase, light-dependent NADPH:Pchlide oxidoreductase, light-dependent NADPH:protochlorophyllide oxidoreductase, light-dependent Pchlide oxidoreductase, Light-dependent protochlorophyllide oxidoreductase, light-driven enzyme protochlorophyllide oxidoreductase, light-independent (dark) Pchlide oxidoreductase, light-independent NADPH:protochlorophyllide oxidoreductase, light-independent protochlorophyllide oxidoreductase, LIPOR, LPOR, NADPH Pchlide oxidoreductase, NADPH-Pchlide oxidoreductase, NADPH-protochlorophyllide oxidoreductase, NADPH-protochlorophyllide oxidoreductase (POR)-like protein, NADPH-protochlorophyllide oxidoreductase A, NADPH-protochlorophyllide oxidoreductase B, NADPH-protochlorophyllide reductase, NADPH2-protochlorophyllide oxidoreductase, NADPH: protochlorophyllide oxidoreductase, NADPH: protochlorophyllide oxidoreductase A, NADPH: protochlorophyllide oxidoreductase B, NADPH:Pchlide oxidoreductase, NADPH:Pchlide oxidoreductase A, NADPH:protochlorophyllide (Pchlide) oxidoreductase, NADPH:protochlorophyllide oxidoreductase, NADPH:protochlorophyllide oxidoreductase A, NADPH:protochlorophyllide oxidoreductase B, Os04g58200, Os10g0496900, OsPORA, OsPORB, PAR-A, Pchilde reductase, Pchlide oxidoreductase, PCR, POR, POR A, POR B, POR C, POR pPm1, POR pPm2, POR-A, POR-B, POR-C, POR-PChlide640, POR-PChlide650, POR1, POR2, POR3, PORA, PORB, PORC, protochlorophyllide oxidoreductase, protochlorophyllide oxidoreductase A, protochlorophyllide oxidoreductase B, protochlorophyllide oxidoreductase C, protochlorophyllide oxidoreductase POR-PChlide640, protochlorophyllide oxidoreductase POR-PChlide650, protochlorophyllide photooxidoreductase, protochlorophyllide reductase
ECTree
Localization
Localization on EC 1.3.1.33 - protochlorophyllide reductase
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PORA precursor, pPORA
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isoform POR1
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nuclear-encoded cytoplasmically sythesized, posttranslationally processed on import into plastids
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nuclear-encoded cytoplasmically sythesized, posttranslationally processed on import into plastids
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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membrane bound
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etioplast internal membrane
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etioplast membrane
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etioplast membrane
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prolamellar body
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from prolamellar body to stroma of etioplast
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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the enzyme (LPOR) exists as a ternary complex of protochlorophyllidee-NADPH-LPOR to form paracrystalline prolamellar bodies (PLBs) in etioplasts
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the enzyme (LPOR) exists as a ternary complex of protochlorophyllidee-NADPH-LPOR to form paracrystalline prolamellar bodies (PLBs) in etioplasts
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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etioplast internal membrane
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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peripheral membrane protein
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contains two photochemically active forms of the enzyme: protochlorophyllide oxidoreductase POR-PChlide640 and POR-PChlide650. Resuspension of prolamellar bodies in media with a pH below 6.8 leads to a rapid conversuion of POR-PChlide650 to POR-PChlide 640 and a dramatic reorganization of the membrane system of the prolamellar body. The disappearence of POR-PChlide 650 and the reorganization of the prolamellar body are irreversible
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associated with
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LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
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LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
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LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
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LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
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LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
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LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
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nucleus-encoded enzyme is synthesized as a larger precursor in the cytosol and imported into the plastid in a substrate-dependent manner. Plastid envelope membrane proteins, called protochlorophyllide-dependent translocon proteins, Ptcs, interact with pPORA during import. Partial suppression of pPORB import in white light
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import of isoform PorA into plastids of cotyledons is substrate-dependent and organ-specific
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plastid membrane
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outside the plastid in the area of the plasmalemma
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inner plastid membrane
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plastid membrane-associated
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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thylakoid-membrane-bound
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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