1.14.15.17: pheophorbide a oxygenase
This is an abbreviated version!
For detailed information about pheophorbide a oxygenase, go to the full flat file.
Word Map on EC 1.14.15.17
-
1.14.15.17
-
chlorophyll
-
catabolite
-
ripening
-
chlorophyllase
-
stay-green
-
macrocycle
-
tetrapyrrole
-
pheophytinase
-
colorless
-
degreening
-
dark-induced
-
phototoxic
-
rieske
-
nonfluorescent
-
thermospermine
-
rieske-type
-
pheophytin
- 1.14.15.17
- chlorophyll
- catabolite
-
ripening
- chlorophyllase
-
stay-green
-
macrocycle
- tetrapyrrole
-
pheophytinase
-
colorless
-
degreening
-
dark-induced
-
phototoxic
-
rieske
-
nonfluorescent
- thermospermine
-
rieske-type
- pheophytin
Reaction
Synonyms
accelerated cell death 1, ACD1, AtPaO, chloroplast pheophorbide a oxygenase PaO1, chloroplast pheophorbide a oxygenase PaO2, CitPaO, EC 1.14.12.20, lethal leaf spot protein LLS1, lethal leaf-spot 1 homolog, Lls1, PAO, pheide a monooxygenase, pheide a oxygenase, pheophorbide a oxygenase
ECTree
Advanced search results
Localization
Localization on EC 1.14.15.17 - pheophorbide a oxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PaO is localized in the chloroplast inner envelope
Q10RT5
integral enzyme, the enzyme contains two putative transit peptides at its N-terminus, which are essential for its functionality, suggesting that targeting of the enzyme to the chloroplast is likely mediated by a putative bipartite transit peptide. Once the precursors of luminal proteins reach the stroma, the first transit peptide for the chloroplast envelop is cleaved off by the stroma processing proteases, and then the intermediate precursor lacking the first transit peptide is translocated into the thylakoid lumen through the second transit peptide
-
integral enzyme, the enzyme contains two putative transit peptides at its N-terminus, which are essential for its functionality, suggesting that targeting of the enzyme to the chloroplast is likely mediated by a putative bipartite transit peptide. Once the precursors of luminal proteins reach the stroma, the first transit peptide for the chloroplast envelop is cleaved off by the stroma processing proteases, and then the intermediate precursor lacking the first transit peptide is translocated into the thylakoid lumen through the second transit peptide
-
the enzyme contains a chloroplast transit peptide