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Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold. [1]. 7578111. Crystal structure of glycosomal glyceraldehyde-3-phosphate. dehydrogenase from Leishmania mexicana: implications for. structure-based drug design and a new position for the inorganic. phosphate binding site.. Kim H, Feil IK, Verlinde CL, Petra PH, Hol WG;. Biochemistry 1995;34:14975-14986. (from Pfam)
glyceraldehyde 3-phosphate dehydrogenase NAD-binding domain-containing protein
GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold. [1]. 7578111. Crystal structure of glycosomal glyceraldehyde-3-phosphate. dehydrogenase from Leishmania mexicana: implications for. structure-based drug design and a new position for the inorganic. phosphate binding site.. Kim H, Feil IK, Verlinde CL, Petra PH, Hol WG;. Biochemistry 1995;34:14975-14986. (from Pfam)
erythrose-4-phosphate dehydrogenase
erythrose-4-phosphate dehydrogenase catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate
This HMM represents the small clade of dehydrogenases in gamma-proteobacteria which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose [1]. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species.
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