E4PD_CROS8
ID E4PD_CROS8 Reviewed; 339 AA.
AC A7MJQ2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=ESA_00408;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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}.
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; CP000783; ABU75706.1; -; Genomic_DNA.
DR RefSeq; WP_004385647.1; NC_009778.1.
DR AlphaFoldDB; A7MJQ2; -.
DR SMR; A7MJQ2; -.
DR EnsemblBacteria; ABU75706; ABU75706; ESA_00408.
DR KEGG; esa:ESA_00408; -.
DR HOGENOM; CLU_030140_0_0_6; -.
DR OMA; NAKVLAW; -.
DR OrthoDB; 944149at2; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000000260; 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.
FT CHAIN 1..339
FT /note="D-erythrose-4-phosphate dehydrogenase"
FT /id="PRO_1000069895"
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 81
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 339 AA; 37294 MW; 8BB904713F20EAF5 CRC64;
MTLRVAINGF GRIGRNVVRA LYESGRRAEI SVVAINELAD AAGMAHLLKY DTSHGRFAWD
VRQEGEQLWI GNDVIRLLHE RDINALPWKA LDVDVVLDCT GVYGSRADGI AHLEAGARKV
LFSHPGGNDL DATVVYGVNE EELRAEHRIV SNASCTTNCI IPIIKLMDDA FGIESGTVTT
IHSAMHDQQV IDAYHPDLRR TRAASQSIIP VDTRLAAGIT RIFPKFHDRF EAIAVRVPTI
NVTAIDLSVT VQKPVKAYEV NLLLQKAAQG AFHGIVDYTE LPLVSTDFNH DPHSAIVDGT
QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMAAIGFR
