1.3.7.12: red chlorophyll catabolite reductase
This is an abbreviated version!
For detailed information about red chlorophyll catabolite reductase, go to the full flat file.
Word Map on EC 1.3.7.12
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1.3.7.12
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oxygenase
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pheophorbide
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pao
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macrocycle
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porphyrin
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pheide
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chlorophyllase
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colorless
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pheophytinase
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phototoxic
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nonfluorescent
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light-dependent
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ferredoxin-dependent
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dark-induced
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stay-green
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bilin
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degreening
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chl-binding
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postharvest
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agriculture
- 1.3.7.12
- oxygenase
- pheophorbide
- pao
-
macrocycle
- porphyrin
-
pheide
- chlorophyllase
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colorless
-
pheophytinase
-
phototoxic
-
nonfluorescent
-
light-dependent
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ferredoxin-dependent
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dark-induced
-
stay-green
-
bilin
-
degreening
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chl-binding
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postharvest
- agriculture
Reaction
+ 2 oxidized ferredoxin [iron-sulfur] cluster = + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
Synonyms
ACD2 protein, At-RCCR, AtRCCR, BoRCCR, BrRCCR, CaRCCR, EC 1.3.1.80, HvRCCR, PHAVU_008G280300g, RCC reductase, RCCR, RCCR-1, RCCR-2, red Chl catabolite reductase, red chlorophyll catabolite reductase, red-chlorophyll-catabolite reductase
ECTree
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Subunits
Subunits on EC 1.3.7.12 - red chlorophyll catabolite reductase
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x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE
homodimer
additional information
2 * 32000, predicted by amino acid sequence, each subunit folds in an alpha/beta/alpha sandwich
homodimer
RCCR folds into a characteristic alphabetaalpha sandwich
RCCR folds into a characteristic alpha/beta/alpha sandwich, similar to that observed in the ferredoxin-dependent bilin reductase family, structure comparisosns, overview
additional information
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RCCR folds into a characteristic alpha/beta/alpha sandwich, similar to that observed in the ferredoxin-dependent bilin reductase family, structure comparisosns, overview
additional information
enzyme RCCR forms a homodimer, in which each subunit folds in an alphabetaalpha sandwich, five N-terminal alpha-helices (H1/H2/H3/H5/H7), an anti-parallel beta-sheet consisting of eight strands (S1-S8), and four C-terminal alpha-helices (H4/H6/H8/H9). The two subunits are related by noncrystallographic 2fold symmetry in which the alpha-helices near the edge of the beta-sheet unique in RCCR participate in intersubunit interaction. The putative RCC-binding site forms an open pocket surrounded by conserved residues among RCCRs. Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis. Primary structure comparisons, overview
additional information
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enzyme RCCR forms a homodimer, in which each subunit folds in an alphabetaalpha sandwich, five N-terminal alpha-helices (H1/H2/H3/H5/H7), an anti-parallel beta-sheet consisting of eight strands (S1-S8), and four C-terminal alpha-helices (H4/H6/H8/H9). The two subunits are related by noncrystallographic 2fold symmetry in which the alpha-helices near the edge of the beta-sheet unique in RCCR participate in intersubunit interaction. The putative RCC-binding site forms an open pocket surrounded by conserved residues among RCCRs. Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis. Primary structure comparisons, overview