ID   E4PD_IDILO              Reviewed;         341 AA.
AC   Q5QVL6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=IL2213;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV83045.1; -; Genomic_DNA.
DR   RefSeq; WP_011235440.1; NC_006512.1.
DR   AlphaFoldDB; Q5QVL6; -.
DR   SMR; Q5QVL6; -.
DR   STRING; 283942.IL2213; -.
DR   EnsemblBacteria; AAV83045; AAV83045; IL2213.
DR   KEGG; ilo:IL2213; -.
DR   eggNOG; COG0057; Bacteria.
DR   HOGENOM; CLU_030140_0_0_6; -.
DR   OMA; NAKVLAW; -.
DR   OrthoDB; 944149at2; -.
DR   UniPathway; UPA00244; UER00309.
DR   Proteomes; UP000001171; 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: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; 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   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.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..341
FT                   /note="D-erythrose-4-phosphate dehydrogenase"
FT                   /id="PRO_0000293150"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         14..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         156..158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         215..216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   BINDING         320
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT   SITE            184
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
SQ   SEQUENCE   341 AA;  37680 MW;  5E307654A8D8D1B8 CRC64;
     MSEPARIAIN GFGRIGRSFL RALYENGYRD SVQVVLINEP AASEAIAHLL KYDSSHGRFG
     EKVTQSGDAL TVAGDNIALT HQTEIEAIDW RAHEVDFVVD CTGVFGSQAD GQLYLQQGVK
     RVLFSHPGKP DVDFTAIYGV NEKELTVDHK VVSNGSCTTN CIVPVIKVLD DAFGIDSGAI
     TTIHSAMHDQ QVIDAYHPDL RRTRAAGRSI IPVDTRLARG IERILPHLEG RFEAIAVRVP
     TTNVTAMDLS VTLNSDATIE QINQVLREQS ERQLAGILDY TEEPLVSIDF NHDPHSSIVD
     GTQTRVSHKR LVKLLCWCDN EWGFANRLLD TAKTMAEQTE H