P-loop containing nucleotide triphosphate hydrolases
P-loop containing nucleoside triphosphate hydrolases
May affect the post-translational activation and/or assembly of the oligomeric structure of RuBisCO.
Belongs to the CbbQ/NirQ/NorQ/GpvN family.
Fructose-1,6-Bisphosphatase, subunit A, domain 1
SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC
D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1
Ribulose bisphosphate carboxylase, large subunit, C-terminal domain
RuBisCO large subunit, N-terminal domain
RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
RuBisCO, large subunit, small (N-terminal) domain
Ribulose bisphosphate carboxylase large chain
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
Heterohexadecamer of 8 large chains and 8 small chains.
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.
Belongs to the RuBisCO large chain family. Type I subfamily.
Ribulose bisphosphate carboxylase, small subunit
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1, CHLOROPLASTIC
Ribulose bisphosphate carboxylase small subunit
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
Heterohexadecamer of 8 large and 8 small subunits.
Belongs to the RuBisCO small chain family.
L-cysteine S-thiosulfotransferase subunit SoxA
Thiosulfate-oxidizing multienzyme system protein SoxA
C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.