ID E4PD_SHELP Reviewed; 338 AA. AC A3QAX7; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 111. DE RecName: Full=D-erythrose-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01640}; DE Short=E4PDH {ECO:0000255|HAMAP-Rule:MF_01640}; DE EC=1.2.1.72 {ECO:0000255|HAMAP-Rule:MF_01640}; GN Name=epd {ECO:0000255|HAMAP-Rule:MF_01640}; GN OrderedLocusNames=Shew_0753; OS Shewanella loihica (strain ATCC BAA-1088 / PV-4). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Shewanellaceae; Shewanella. OX NCBI_TaxID=323850; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1088 / PV-4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G., RA Fredrickson J., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella loihica PV-4."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4- CC phosphate to 4-phosphoerythronate. {ECO:0000255|HAMAP-Rule:MF_01640}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-erythrose 4-phosphate + NAD(+) + H2O = 4-phospho-D- CC erythronate + NADH + 2 H(+); 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 Evidence={ECO:0000255|HAMAP-Rule:MF_01640}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5. CC {ECO:0000255|HAMAP-Rule:MF_01640}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01640}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01640}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. Epd subfamily. {ECO:0000255|HAMAP-Rule:MF_01640}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000606; ABO22625.1; -; Genomic_DNA. DR RefSeq; WP_011864559.1; NC_009092.1. DR AlphaFoldDB; A3QAX7; -. DR SMR; A3QAX7; -. DR STRING; 323850.Shew_0753; -. DR KEGG; slo:Shew_0753; -. DR eggNOG; COG0057; Bacteria. DR HOGENOM; CLU_030140_0_2_6; -. DR OrthoDB; 9803304at2; -. DR UniPathway; UPA00244; UER00309. DR Proteomes; UP000001558; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0042823; P:pyridoxal 5'-phosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd23937; GAPDH_C_E4PDH; 1. DR CDD; cd17892; GAPDH_N_E4PDH; 1. DR FunFam; 3.30.360.10:FF:000007; D-erythrose-4-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_01640; E4P_dehydrog; 1. DR InterPro; IPR006422; E4P_DH_bac. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01532; E4PD_g-proteo; 1. DR NCBIfam; TIGR01534; GAPDH-I; 1. DR NCBIfam; NF010058; PRK13535.1; 1. DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis; KW Reference proteome. FT CHAIN 1..338 FT /note="D-erythrose-4-phosphate dehydrogenase" FT /id="PRO_0000293163" FT ACT_SITE 154 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" FT BINDING 11..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" FT BINDING 153..155 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" FT BINDING 199 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" FT BINDING 212..213 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" FT BINDING 235 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" FT BINDING 317 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" FT SITE 181 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640" SQ SEQUENCE 338 AA; 37201 MW; 0F99C35301D06BD0 CRC64; MIKVAINGYG RIGRSILRAL YESGKRDQIQ IVAINELANP EAMLHLTQYD TTHGRFQSPA SLDANVMTIG DDRIQLLHEA DAEKLPWRSL DIDIVFEATG ALIDRQACEA HIRAGAKQVL ISHPSSGDVD ATIVYGVNHQ DLKAEHKVVS NASCTTNCLV PIIQVLDRAF KVRSGAITTI HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPEMKDKFE AISVRVPTIN VTAIDLSVTL DKRVDIDTVN QVLSQAANGS YQGVVGYTNA PLVSCDFNHD PRSSIVDGTQ TRVSDGHLVK LLLWCDNEWG FANRMLDTSL EMIKAVRA //