ID E5B1W8_ERWAM Unreviewed; 348 AA.
AC E5B1W8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE RecName: Full=D-erythrose-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01640};
DE Short=E4PDH {ECO:0000256|HAMAP-Rule:MF_01640};
DE EC=1.2.1.72 {ECO:0000256|HAMAP-Rule:MF_01640};
GN Name=epd {ECO:0000256|HAMAP-Rule:MF_01640,
GN ECO:0000313|EMBL:CBX79469.1};
GN ORFNames=EAIL5_0649 {ECO:0000313|EMBL:CBX79469.1};
OS Erwinia amylovora ATCC BAA-2158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX79469.1};
RN [1] {ECO:0000313|EMBL:CBX79469.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX79469.1};
RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT Restricted to Rubus Plants.";
RL J. Bacteriol. 193:785-786(2011).
CC -!- FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4-
CC phosphate to 4-phosphoerythronate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01640}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01640}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01640}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. Epd subfamily. {ECO:0000256|HAMAP-Rule:MF_01640}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01640}.
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DR EMBL; FR719186; CBX79469.1; -; Genomic_DNA.
DR AlphaFoldDB; E5B1W8; -.
DR UniPathway; UPA00244; UER00309.
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 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 PANTHER; PTHR43148:SF3; D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01640};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01640};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01640};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096, ECO:0000256|HAMAP-
KW Rule:MF_01640}.
FT DOMAIN 3..155
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 155
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 154..156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 213..214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 182
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01640,
FT ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 348 AA; 38039 MW; FD6F1DE35179074D CRC64;
MTVRIAINGF GRIGRNVLRA LYETGRRAEI TVVAINELAD AAGMAHLLKY DTSHGRFAWD
VRQERDLLTV GDDAIRLLHI PEIHTLPWRE LNVDIVLDCT GVYGSRADGE AHLKAGARKV
LFSHPGGHDL DATVVYGVNE KELLPEHLLV SNASCTTNCI IPIIKLLDDA WGIESGTVTT
IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTRLAAGIT RIFPKFNDRF EAIAVRVPTI
NVTAIDLSVS VRDAVKACEV NALLHSASVG AFNGIVDYTE LPLVSIDFNH DPHSAIVDGT
QTRVSGQHLI KTLVWCDNEW GFANRMIDTT LAMASSGFSQ DAAASIKL
//
