AC MF_01640; DC Protein; auto TR HAMAP; MF_01640; -; 1; level=0 XX Names: E4P_dehydrog XX ID E4PD DE RecName: Full=D-erythrose-4-phosphate dehydrogenase; DE Short=E4PDH; DE EC=1.2.1.72; GN Name=epd; XX CC -!- FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4- CC phosphate to 4-phosphoerythronate. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-erythrose 4-phosphate + H2O + NAD(+) = 4-phospho-D- CC erythronate + 2 H(+) + NADH; Xref=Rhea:RHEA:12056, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16897, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58766; EC=1.2.1.72; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. Epd subfamily. XX DR PROSITE; PS00071; GAPDH; 1; trigger=no DR Pfam; PF02800; Gp_dh_C; 1; trigger=no DR Pfam; PF00044; Gp_dh_N; 1; trigger=no DR PRINTS; PR00078; G3PDHDRGNASE; 1; trigger=no DR NCBIfam; TIGR01532; E4PD_g-proteo; 1; trigger=no XX KW Cytoplasm KW NAD KW Oxidoreductase KW Pyridoxine biosynthesis XX GO GO:0048001; F:erythrose-4-phosphate dehydrogenase activity GO GO:0042823; P:pyridoxal phosphate biosynthetic process GO GO:0008615; P:pyridoxine biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: E4PD_ECOLI (P0A9B6) FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: R-[IV] FT BINDING 154..156 FT /ligand="substrate" FT Condition: S-C-T FT BINDING 213..214 FT /ligand="substrate" FT Condition: T-[KR] FT ACT_SITE 155 FT /note="Nucleophile" FT Condition: C FT BINDING 81 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: R FT BINDING 200 FT /ligand="substrate" FT Optional; Condition: R FT BINDING 236 FT /ligand="substrate" FT Optional; Condition: R FT BINDING 318 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: N FT SITE 182 FT /note="Activates thiol group during catalysis" FT Condition: H XX Size: 336-371; Related: None; Template: P0A9B6; Scope: Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.24 2023/06/01 //