ID E3G486_ENTLS Unreviewed; 339 AA.
AC E3G486;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=Entcl_0827 {ECO:0000313|EMBL:ADO47101.1};
OS Enterobacter lignolyticus (strain SCF1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO47101.1, ECO:0000313|Proteomes:UP000006872};
RN [1] {ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA Hazen T.C., Woyke T.;
RT "Complete sequence of Enterobacter cloacae SCF1.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO47101.1, ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|EMBL:ADO47101.1,
RC ECO:0000313|Proteomes:UP000006872};
RX PubMed=22180812; DOI=10.4056/sigs.2104875;
RA Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL Stand. Genomic Sci. 5:69-85(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}.
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DR EMBL; CP002272; ADO47101.1; -; Genomic_DNA.
DR RefSeq; WP_013364853.1; NC_014618.1.
DR AlphaFoldDB; E3G486; -.
DR STRING; 701347.Entcl_0827; -.
DR KEGG; esc:Entcl_0827; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_6; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000006872; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000006872}.
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 81
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 339 AA; 37046 MW; 4DB7D1EC8BD5BB36 CRC64;
MTVRVAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGIAHLLKY DTSHGRFAWD
VRQDREQLFV GDDAIRLLHE RSIDALPWSE LNIDVVLDCT GVYGSRADGE AHLAAGARKV
LFSHPGGNDL DATVVYGVNH DQLAPEHRIV SNASCTTNCI IPVIKLLDDA WGIESGTVTT
IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTKLAAGIT RIFPQFNDRF EAIAVRVPTI
NVTAIDLSVT VKKPVKACEV NALLQKAALG AFHGIVDYTE LPLVSTDFNH DPHSAIVDGT
QTRVSGSHLI KTLVWCDNEW GFANRMLDTT LAMAAQGFR
//
