E4PD_AERS4
ID E4PD_AERS4 Reviewed; 336 AA.
AC A4SRF2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=ASA_3506;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(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; CP000644; ABO91474.1; -; Genomic_DNA.
DR RefSeq; WP_005318807.1; NC_009348.1.
DR AlphaFoldDB; A4SRF2; -.
DR SMR; A4SRF2; -.
DR STRING; 382245.ASA_3506; -.
DR EnsemblBacteria; ABO91474; ABO91474; ASA_3506.
DR KEGG; asa:ASA_3506; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_0_6; -.
DR OMA; NAKVLAW; -.
DR OrthoDB; 944149at2; -.
DR UniPathway; UPA00244; UER00309.
DR Proteomes; UP000000225; 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.
FT CHAIN 1..336
FT /note="D-erythrose-4-phosphate dehydrogenase"
FT /id="PRO_0000293144"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 153..155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT BINDING 317
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
FT SITE 181
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01640"
SQ SEQUENCE 336 AA; 36786 MW; E8921487B5FB191C CRC64;
MIKIAINGYG RIGRNVLRAL YESGRDKNIK IVAINELAAP EAMVHLTRFD TSHGRFRYPV
QLAGHSMLVG EDLISLFAEQ DPANLPWRAL GVDVVLDCTG VFGSRADAEL HLGAGAGKVL
FSHPADADVD ATIVYGVNHQ VLTGRERIVS NASCTTNCVV PVIETLHREF EINCGTITTI
HSAMHDQQVI DAYHSDLRRT RAASQSIIPV DTKLAKGLER ILPHFAGKFE AIAVRVPTIN
VTAMDLSITV RKKVTVTDVN QALQRASRGT LSGILDYTEE PLVSVDFNHD AHSCIIDGTQ
TRVSDANLVK MLMWCDNEWG FANRMLDTTR AMMAAG
