ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [Gracilariopsis cf. lemaneiformis]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
RuBisCO_large super family | cl08232 | Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ... |
1-17 | 5.96e-06 | ||
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions. The actual alignment was detected with superfamily member CHL00040: Pssm-ID: 471793 Cd Length: 475 Bit Score: 39.30 E-value: 5.96e-06
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Name | Accession | Description | Interval | E-value | ||
rbcL | CHL00040 | ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit |
1-17 | 5.96e-06 | ||
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit Pssm-ID: 176981 Cd Length: 475 Bit Score: 39.30 E-value: 5.96e-06
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RuBisCO_large_I | cd08212 | Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ... |
1-15 | 8.87e-05 | ||
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form I is the most abundant class, present in plants, algae, and bacteria, and forms large complexes composed of 8 large and 8 small subunits. Pssm-ID: 173977 Cd Length: 450 Bit Score: 35.86 E-value: 8.87e-05
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Name | Accession | Description | Interval | E-value | ||
rbcL | CHL00040 | ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit |
1-17 | 5.96e-06 | ||
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit Pssm-ID: 176981 Cd Length: 475 Bit Score: 39.30 E-value: 5.96e-06
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RuBisCO_large_I | cd08212 | Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ... |
1-15 | 8.87e-05 | ||
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form I is the most abundant class, present in plants, algae, and bacteria, and forms large complexes composed of 8 large and 8 small subunits. Pssm-ID: 173977 Cd Length: 450 Bit Score: 35.86 E-value: 8.87e-05
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rbcL | PRK04208 | ribulose bisophosphate carboxylase; Reviewed |
1-16 | 3.75e-04 | ||
ribulose bisophosphate carboxylase; Reviewed Pssm-ID: 179787 Cd Length: 468 Bit Score: 34.11 E-value: 3.75e-04
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Blast search parameters | ||||
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