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Annotation rule MF_01640
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General rule information [?]

Accession MF_01640
Dates 11-JUN-2007 (Created)
27-OCT-2018 (Last updated, Version 18)
Name E4P_dehydrog
Scope
Bacteria; Proteobacteria
Template P0A9B6 (E4PD_ECOLI)

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
epd

Comments [?]

Function Catalyzes 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;.
Pathway Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5.
Subunit Homotetramer.
Subcellular location Cytoplasm.
Similarity Belongs 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;
PF00044; Gp_dh_N; 1;
PRINTS PR00078; G3PDHDRGNASE; 1;
TIGRFAMs TIGR01532; E4PD_g-proteo; 1;

Features [?]

From: E4PD_ECOLI (P0A9B6)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     12     13       NAD     R-[IV]  
REGION     154     156       Substrate binding     S-C-T  
REGION     213     214       Substrate binding     T-[KR]  
ACT_SITE     155     155       Nucleophile     C  
BINDING (Optional)     81     81       NAD; via carbonyl oxygen     R  
BINDING (Optional)     200     200       Substrate     R  
BINDING (Optional)     236     236       Substrate     R  
BINDING (Optional)     318     318       NAD     N  
SITE     182     182       Activates thiol group during catalysis     H  

Additional information [?]

Size range 336-371 amino acids
Related rules None
Fusion None