ID   E4PD_ERWT9              Reviewed;         348 AA.
AC   B2VF24;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=ETA_28150;
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO97861.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2VF24; -.
DR   SMR; B2VF24; -.
DR   STRING; 465817.ETA_28150; -.
DR   EnsemblBacteria; CAO97861; CAO97861; ETA_28150.
DR   KEGG; eta:ETA_28150; -.
DR   eggNOG; COG0057; Bacteria.
DR   HOGENOM; CLU_030140_0_2_6; -.
DR   OMA; NAKVLAW; -.
DR   UniPathway; UPA00244; UER00309.
DR   Proteomes; UP000001726; 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; 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   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   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Pyridoxine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..348
FT                   /note="D-erythrose-4-phosphate dehydrogenase"
FT                   /id="PRO_1000186828"
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         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;  37873 MW;  16BAC701EFF292FC CRC64;
     MTVRIAINGF GRIGRNVLRA LYETGRRAEI SAVAINELAD AAGMAHLLKY DTSHGRFAWD
     VRQERDLLTV GDDTIRLLHI PEIGSLPWRE LNVDIVLDCT GVYGSRADGE AHLKAGARKV
     LFSHPGGHDL DATVVYGVNE KELLPEHLLV SNASCTTNCI IPIIKLLDDA WGIESGTVTT
     IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTRLAAGIT RIFPKFNDRF EAIAVRVPTI
     NVTAIDLSVS VRDAVKASEV NALLHSASLG AFSGIVDYTE LPLVSIDFNH DPHSAIVDGT
     QTRVSGQHLI KTLVWCDNEW GFANRMIDTT LAMAASGFSL DAAASIKL