Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803.
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Gap2 was cloned by complementing an E. coli gap mutant; native and recombinant Gap2 are homotetramers with dual NAD/NADP specificity.
"The recombinant GAPDH2 showed the dual pyridine nucleotide specificity characteristic of the native cyanobacterial enzyme"
Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803.
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gap2 mutants cannot grow photoautotrophically or on organic acids, but grow on glucose; Gap2 functions in the Calvin cycle and gluconeogenesis, Gap1 in glycolysis.
"While Gap2 operates in the photosynthetic Calvin cycle and in non-photosynthetic gluconeogenesis, Gap1 seems to be essential only for glycolytic glucose breakdown"
Evolutionary conserved light regulation of Calvin cycle activity by NADPH-mediated reversible phosphoribulokinase/CP12/ glyceraldehyde-3-phosphate dehydrogenase complex dissociation.
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Synechocystis GAPDH forms an NADPH-dissociable complex with CP12 and phosphoribulokinase.
"light regulation of Calvin cycle activity via NADPH-mediated reversible phosphoribulokinase/CP12/GAPDH complex dissociation is conserved in all photosynthetic organisms"
CP12 fine-tunes the Calvin-Benson cycle and carbohydrate metabolism in cyanobacteria.
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GapDH2 (Sll1342)-eYFP forms CP12-dependent complexes with PRK in the dark in living Synechocystis cells.
"These results show for the first time the CP12-dependent complex formation with GapDH2 or PRK during light/dark transitions inside living Synechocystis cells."
The primary carbon metabolism in cyanobacteria and its regulation.
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Review summarizing that GapDH2 functions mainly in the CBB cycle using NADPH, while NADH-specific GapDH1 is active in darkness or low light when GapDH2 is inhibited by Cp12.
"In low photosynthetic activity in darkness or low light, GapDH1 is the active GapDH isoenzyme which only utilises NADH, while GapDH2 is inhibited by Cp12."
Functional characterization of GAPDH2 through overexpression and dsRNA-mediated RNA interference in Synechocystis.