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Literature summary for 1.3.1.33 extracted from
- Evolution of light-independent protochlorophyllide oxidoreductase (2019), Protoplasma, 256, 293-312 .
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protochlorophyllide + NADPH + H+ | Dinoroseobacter shibae | - |
chlorophyllide a + NADP+ | - |
r |  |
| protochlorophyllide + NADPH + H+ | Gemmatimonas phototrophica | - |
chlorophyllide a + NADP+ | - |
r | |
| protochlorophyllide + NADPH + H+ | Erythrobacter litoralis | - |
chlorophyllide a + NADP+ | - |
r | |
| protochlorophyllide + NADPH + H+ | Limnohabitans sp. 15K | - |
chlorophyllide a + NADP+ | - |
r | |
| protochlorophyllide + NADPH + H+ | Dinoroseobacter shibae DFL12 | - |
chlorophyllide a + NADP+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Dinoroseobacter shibae | A8LUF3 | - |
- |
| Dinoroseobacter shibae DFL12 | A8LUF3 | - |
- |
| Erythrobacter litoralis | A0A074MWM0 | - |
- |
| Gemmatimonas phototrophica | A0A143BMX6 | - |
- |
| Limnohabitans sp. 15K | A0A2M6VWJ9 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protochlorophyllide + NADPH + H+ | - |
Dinoroseobacter shibae | chlorophyllide a + NADP+ | - |
r | |
| protochlorophyllide + NADPH + H+ | - |
Gemmatimonas phototrophica | chlorophyllide a + NADP+ | - |
r | |
| protochlorophyllide + NADPH + H+ | - |
Erythrobacter litoralis | chlorophyllide a + NADP+ | - |
r | |
| protochlorophyllide + NADPH + H+ | - |
Limnohabitans sp. 15K | chlorophyllide a + NADP+ | - |
r | |
| protochlorophyllide + NADPH + H+ | - |
Dinoroseobacter shibae DFL12 | chlorophyllide a + NADP+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| B9Z40_03660 | - |
Limnohabitans sp. 15K |
| EH32_03160 | - |
Erythrobacter litoralis |
| GEMMAAP_15250 | - |
Gemmatimonas phototrophica |
| Light-dependent protochlorophyllide oxidoreductase | - |
Dinoroseobacter shibae |
| Light-dependent protochlorophyllide oxidoreductase | - |
Gemmatimonas phototrophica |
| Light-dependent protochlorophyllide oxidoreductase | - |
Erythrobacter litoralis |
| Light-dependent protochlorophyllide oxidoreductase | - |
Limnohabitans sp. 15K |
| LPOR | - |
Dinoroseobacter shibae |
| LPOR | - |
Gemmatimonas phototrophica |
| LPOR | - |
Erythrobacter litoralis |
| LPOR | - |
Limnohabitans sp. 15K |
| protochlorophyllide reductase | - |
Dinoroseobacter shibae |
| protochlorophyllide reductase | - |
Gemmatimonas phototrophica |
| protochlorophyllide reductase | - |
Erythrobacter litoralis |
| protochlorophyllide reductase | - |
Limnohabitans sp. 15K |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Dinoroseobacter shibae | |
| NADP+ | - |
Gemmatimonas phototrophica | |
| NADP+ | - |
Erythrobacter litoralis | |
| NADP+ | - |
Limnohabitans sp. 15K | |
| NADPH | - |
Dinoroseobacter shibae | |
| NADPH | - |
Gemmatimonas phototrophica | |
| NADPH | - |
Erythrobacter litoralis | |
| NADPH | - |
Limnohabitans sp. 15K | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Limnohabitans sp. 15K |
| 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 | Dinoroseobacter shibae |
| 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 | Gemmatimonas phototrophica |
| 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 | Erythrobacter litoralis |
| metabolism | the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase | Dinoroseobacter shibae |
| metabolism | the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase | Erythrobacter litoralis |
| metabolism | the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase | Limnohabitans sp. 15K |
| metabolism | the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by lightdependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase | Gemmatimonas phototrophica |
| additional information | 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 | Dinoroseobacter shibae |
| additional information | 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 | Gemmatimonas phototrophica |
| additional information | 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 | Erythrobacter litoralis |
| additional information | 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 | Limnohabitans sp. 15K |
| physiological function | the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR | Dinoroseobacter shibae |
| physiological function | the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR | Gemmatimonas phototrophica |
| physiological function | the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR | Erythrobacter litoralis |
| physiological function | the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR | Limnohabitans sp. 15K |
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