EC Number   |
General Information |
Reference |
|---|
    1.3.1.33 | more |
a clear distinction of the DPOR and LPOR functions cannot be made as oxygen-sensitive DPOR, which is typically inactivated in the increased oxygen concentration, remains functional in Dinoroseobacter shibae. The TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif,which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity |
-, 763678 |
| 1.3.1.33 | malfunction |
a PORA null mutant (porA-1) and PORA RNAi lines display severe photoautotrophic growth defects, which can be partially rescued on sucrose-supplemented growth media. Elimination of PORA during skotomorphogenesis results in reductions in the volume and frequency of prolamellar bodies, and in photoactive Pchlide conversion |
726185 |
| 1.3.1.33 | evolution |
all modern sequences of light-dependent protochlorophyllide oxidoreductase POR diverged from a single sequence about 1.36 billlion years ago. The LPOR gene was then duplicated at least 10 times in angiosperms, leading to the formation of two or even more LPOR isoforms in multiple species. In the case of Arabidopsis thaliana, isoforms PORA and PORB originated in one duplication event, in contrary to the isoform PORC, which diverged first |
762710 |
| 1.3.1.33 | malfunction |
an enzyme-less mutant grows photoautotrophically in moderate light and contains a maximum of 20% of the wild type chlorophyll level |
726255 |
| 1.3.1.33 | evolution |
DPOR (EC 1.3.7.7) and LPOR (EC 1.3.1.33) initially evolved in the ancestral prokaryotic genome perhaps at different times. DPOR originated in the anoxygenic environment of the Earth from nitrogenase-like enzyme of methanogenic archaea. Due to the transition from anoxygenic to oxygenic photosynthesis in the prokaryote, the DPOR was mostly inactivated in the daytime by photosynthetic O2 leading to the evolution of oxygen-insensitive LPOR that could function in the light. The primary endosymbiotic event transferred the DPOR and LPOR genes to the eukaryotic phototroph, the DPOR remained in the genome of the ancestor that turned into the plastid, whereas LPOR was transferred to the host nuclear genome. Despite the evolution of its nonhomologous isofunctional counterpart LPOR, the DPOR continues to be functional in both oxygenic and anoxygenic photosynthetic organisms. Thus, DPOR was not exactly replaced but supplemented with the LPOR. Limnohabitans sp. strain 15K has acquired LPOR through horizontal gene transfer |
763678 |
| 1.3.1.33 | evolution |
DPOR (EC 1.3.7.7) and LPOR (EC 1.3.1.33) initially evolved in the ancestral prokaryotic genome perhaps at different times. DPOR originated in the anoxygenic environment of the Earth from nitrogenase-like enzyme of methanogenic archaea. Due to the transition from anoxygenic to oxygenic photosynthesis in the prokaryote, the DPOR was mostly inactivated in the daytime by photosynthetic O2 leading to the evolution of oxygen-insensitive LPOR that could function in the light. The primary endosymbiotic event transferred the DPOR and LPOR genes to the eukaryotic phototroph, the DPOR remained in the genome of the ancestor that turned into the plastid, whereas LPOR was transferred to the host nuclear genome. Despite the evolution of its nonhomologous isofunctional counterpart LPOR, the DPOR continues to be functional in both oxygenic and anoxygenic photosynthetic organisms. Thus, DPOR was not exactly replaced but supplemented with the LPOR. LPOR protein phylogeny further corroborates the horizontal gene transfer from cyanobacteria |
-, 763678 |
| 1.3.1.33 | metabolism |
ferredoxin-dependent biliverdin reductase, PCYA1 (EC 1.3.7.5), is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) via its FDBR domain, but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). This interaction is specific to Chlamydomonas since the Arabidopsis thaliana homologous proteins do not interact with each other, yeast two-hybrid and pull down assay analyses of protein-protein interaction |
-, 763107 |
| 1.3.1.33 | physiological function |
in leaf of etiolated seedlings, prolamellar bodies are smaller in the etioplasts of mutant plants than in the wild type. In field-grown seedlings, the chloroplasts in the light-green sectors of mutant leaves exhibit decreased thylakoid stacking with a few plastglobules. PorB is essential for both prolamellar bodies and photoactive protochlorophyllide formation in dark conditions for light-dependent chlorophyll synthesis |
743467 |
| 1.3.1.33 | physiological function |
isoform POR1 supports photoacclimation, whereas isoform POR2 is responsible for daily chlorophyll synthesis |
741255 |
| 1.3.1.33 | malfunction |
it is shown that a porA-1 null mutant (porA mutant) carries a second dissociation insertion in another gene closely linked to the PORA gene that is expected to affect the phenotype of the porA mutant |
726188 |
