ID   E4PD_SHEON              Reviewed;         338 AA.
AC   Q8EIB2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 131.
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=SO_0931;
OS   Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG
OS   19005 / NCIMB 14063 / MR-1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063
RC   / MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54005.1; -; Genomic_DNA.
DR   RefSeq; WP_011071211.1; NC_004347.2.
DR   AlphaFoldDB; Q8EIB2; -.
DR   SMR; Q8EIB2; -.
DR   STRING; 211586.SO_0931; -.
DR   PaxDb; 211586-SO_0931; -.
DR   KEGG; son:SO_0931; -.
DR   PATRIC; fig|211586.12.peg.893; -.
DR   eggNOG; COG0057; Bacteria.
DR   HOGENOM; CLU_030140_0_0_6; -.
DR   OrthoDB; 9803304at2; -.
DR   PhylomeDB; Q8EIB2; -.
DR   BioCyc; SONE211586:G1GMP-868-MONOMER; -.
DR   UniPathway; UPA00244; UER00309.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006006; P:glucose metabolic process; IBA:GO_Central.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01532; E4PD_g-proteo; 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_0000293164"
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;  37241 MW;  FB58AA57643E8006 CRC64;
     MIRVAINGYG RIGRSILRAL YESGKRQQIQ IVAINELAKP EAIIHLTQYD TTHGRFQPRV
     KLVDGQMQIG DDTIKIFHEP DPAKLPWREL DIDIVYEATG AILDRQSCEA HIHAGAKQVL
     ISHPSSADVD GTIVYGVNHD LLRAEHTVVS NASCTTNCIV PVIDVLDKHF GVKSGAITTI
     HSAMNDQQVI DAYHDDLRRT RAAGQSIIPV DTKLARGIER ILPHMKDKFE AISVRVPTIN
     VTAIDLSVTL DKTVDIATVN QVLELAANGR FNGILGYTDE PLVSCDFNHD PRSSIVDGTQ
     TRVSAGQLVK LLLWCDNEWG FANRMLDTSL AMIAAKQS
//