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Literature summary extracted from

  • Xie, Q.; Liang, Y.; Zhang, J.; Zheng, H.; Dong, G.; Qian, Q.; Zuo, J.
    Involvement of a putative bipartite transit peptide in targeting rice pheophorbide a oxygenase into chloroplasts for chlorophyll degradation during leaf senescence (2016), J. Genet. Genomics, 43, 145-154.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.17 gene EAS1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative RT-PCR analysis of EAS1 gene expression in different tissues of rice. Only a short version of EAS1 lacking the first putative transit peptide, but not the full-length EAS1, is capable of rescuing the Arabidopsis acd1 mutant phenotype Oryza sativa Japonica Group

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.17 additional information screening and genotyping for gene eas1 mutants showing an early senescence phenotype, overview. The eas1 mutant is defective in Chl breakdown, which may cause the accumulation of Chl intermediates, leading to the cell death phenotype in light conditions Oryza sativa Japonica Group

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.17 chloroplast membrane 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 Oryza sativa Japonica Group 31969
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Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.17 [2Fe-2S] cluster Rieske domain with a [2Fe-2S] cluster at its N-terminal region that accepts electrons from a reductase, and a functional PaO domain at the carboxyl-terminal region Oryza sativa Japonica Group

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.17 additional information Oryza sativa Japonica Group PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC) ?
-
?
1.14.15.17 additional information Oryza sativa Japonica Group Nipponbare PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC) ?
-
?
1.14.15.17 pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Oryza sativa Japonica Group
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red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
1.14.15.17 pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Oryza sativa Japonica Group Nipponbare
-
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.17 Oryza sativa Japonica Group Q10RT5 nuclear gene EAS1, i.e. early senescence 1
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1.14.15.17 Oryza sativa Japonica Group Nipponbare Q10RT5 nuclear gene EAS1, i.e. early senescence 1
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.15.17 leaf
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Oryza sativa Japonica Group
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1.14.15.17 additional information enzyme expression analysis in different tissues of rice Oryza sativa Japonica Group
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.17 additional information PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC) Oryza sativa Japonica Group ?
-
?
1.14.15.17 additional information PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC) Oryza sativa Japonica Group Nipponbare ?
-
?
1.14.15.17 pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Oryza sativa Japonica Group red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?
1.14.15.17 pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Oryza sativa Japonica Group Nipponbare red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.17 PAO
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Oryza sativa Japonica Group
1.14.15.17 pheophorbide a oxygenase
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Oryza sativa Japonica Group

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.17 Ferredoxin
-
Oryza sativa Japonica Group

General Information

EC Number General Information Comment Organism
1.14.15.17 evolution PaO is an evolutionarily conserved protein, and EAS1 is 68% identical to the Arabidopsis ACCERLERATED CELL DEATH (ACD1) protein Oryza sativa Japonica Group
1.14.15.17 malfunction during the early growth stage (at the 3th leaf stage), eas1 mutants do not show detectable differences compared to wild-type plants. At the heading stage, old leaves of eas1 mutants turn yellowish or brownish, when wild-type plants are still healthy and green. Small chlorotic lesions are first observed near the tip, and then spread down to the entire leaves of eas1 mutants. At the grain filling stage, the leaf senescence phenotype of eas1 is more apparent compared to wild-type, as most eas1 mutant leaves, culms and sheaths turned to dark brown. In addition to the leaf senescence phenotype, the mature eas1 mutant plants also exhibit apparent developmental defects, such as semi-dwarfism, reduced tiller number and partial-filling Oryza sativa Japonica Group
1.14.15.17 physiological function gene EAS1 encodes a PaO enzyme containing a putative bipartite chloroplast-targeting peptide, both of which are genetically important for the function of EAS1 during plant growth and development. Pheophorbide a oxygenase (PaO) is a key enzyme for chlorophyll breakdown and involved in chlorophyll degradation during leaf senescence Oryza sativa Japonica Group