HAMAP logo
Due to maintenance work, this service will be unavailable Tuesday 16 between 06:00 and 06:30 - CEST. Apologies for the inconvenience.

HAMAP rule MF_01640

Send feedback

General rule information [?]

Accession MF_01640
Dates 11-JUN-2007 (Created)
1-JUN-2023 (Last updated, Version 24)
Name E4P_dehydrog
Scope(s) Bacteria
Pseudomonadota
Template(s) P0A9B6 (E4PD_ECOLI); [ Recover all ]
Triggered by HAMAP; MF_01640 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier E4PD
Protein name RecName: Full=D-erythrose-4-phosphate dehydrogenase;
                 Short=E4PDH;
                 EC=1.2.1.72;
Gene name Name=epd;

Comments [?]

FUNCTIONCatalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate.
CATALYTIC ACTIVITY Reaction=D-erythrose 4-phosphate + H2O + NAD(+) = 4-phospho-D- erythronate + 2 H(+) + NADH; Xref=Rhea:RHEA:12056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16897, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58766; EC=1.2.1.72;
PATHWAYCofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5.
SUBUNITHomotetramer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily.

Keywords [?]


Gene Ontology [?]

GO:0048001; Molecular function:erythrose-4-phosphate dehydrogenase activity
GO:0042823; Biological process:pyridoxal phosphate biosynthetic process
GO:0008615; Biological process:pyridoxine biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS00071; GAPDH; 1;
Pfam PF02800; Gp_dh_C; 1;
Pfam PF00044; Gp_dh_N; 1;
PRINTS PR00078; G3PDHDRGNASE; 1;
NCBIfam TIGR01532; E4PD_g-proteo; 1;

Features [?]

From: E4PD_ECOLI (P0A9B6)
Key From To Description Tag Condition FTGroup
BINDING 12 13 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
R-[IV]
BINDING 154 156 /ligand="substrate" S-C-T
BINDING 213 214 /ligand="substrate" T-[KR]
ACT_SITE 155 155 /note="Nucleophile" C
BINDING 81 81 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
R
BINDING 200 200 /ligand="substrate" R
BINDING 236 236 /ligand="substrate" R
BINDING 318 318 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
N
SITE 182 182 /note="Activates thiol group during catalysis" H

Additional information [?]

Size range 336-371 amino acids
Related rules None
Fusion Nter: None Cter: None



View rule in raw text format (no links)