ID   E4PD_SALCH              Reviewed;         348 AA.
AC   Q57K44;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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}; OrderedLocusNames=SCH_3012;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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 + 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         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}.
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DR   EMBL; AE017220; AAX66918.1; -; Genomic_DNA.
DR   RefSeq; WP_000218338.1; NC_006905.1.
DR   AlphaFoldDB; Q57K44; -.
DR   SMR; Q57K44; -.
DR   EnsemblBacteria; AAX66918; AAX66918; SCH_3012.
DR   KEGG; sec:SCH_3012; -.
DR   HOGENOM; CLU_030140_0_0_6; -.
DR   OMA; NAKVLAW; -.
DR   UniPathway; UPA00244; UER00309.
DR   Proteomes; UP000000538; 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 phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR43148; PTHR43148; 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; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01532; E4PD_g-proteo; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis.
FT   CHAIN           1..348
FT                   /note="D-erythrose-4-phosphate dehydrogenase"
FT                   /id="PRO_0000293156"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         12..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         81
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         154..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         213..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         318
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   SITE            182
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
SQ   SEQUENCE   348 AA;  38125 MW;  5009E1EFBB31413A CRC64;
     MTVRIAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWE
     VRHEREQLFV GDDVIRILHE RTLADLPWRE LGVDVVLDCT GVYGNREHGE AHIAAGAKKV
     LFSHPGSNDL DATVVFGVNQ NQLRAEHRIV SNASCTTNCI IPVIKLLDDA YGIESGTVTT
     IHSAMNDQQV IDAYHSDLRR TRAASQSIIP VDTKLAAGIT RIFPQFNDRF EAIAVRVPTI
     NVTAIDLSVT VKKPVKASEV NQLLQKAAQG AFHGIVDYTE SPLVSIDFNH DPHSAIVDGT
     QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMAAVGFRL DASASTKL