D-erythrose-4-phosphate dehydrogenase (P0A9B6)

Identification
Name:D-erythrose-4-phosphate dehydrogenase
Synonyms:
  • E4PDH
Gene Name:epd
Enzyme Class:
Biological Properties
General Function:Involved in erythrose-4-phosphate dehydrogenase activity
Specific Function:Catalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0Water + 1.0NAD ↔ 1.04-Phospho-D-erythronate + 2.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0NAD + 1.0Water ↔ 1.04-Phospho-D-erythronate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+2.0Thumb
1.0D-Erythrose 4-phosphate + 1.0NAD + 1.0Water → 1.04-Phospho-D-erythronate + 1.0NADH + 2.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0Water + 1.0NAD ↔ 1.04-Phospho-D-erythronate + 2.0Hydrogen ion + 1.0NADH
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0NAD + 1.0Water → 1.04-Phospho-D-erythronate + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200954-Phospho-D-erythronateMetaboCard
ECMDB02649D-Erythrose 4-phosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
catalytic activity
erythrose-4-phosphate dehydrogenase activity
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
oxidation reduction
pyridoxal phosphate biosynthetic process
Gene Properties
Blattner:b2927
Gene OrientationCounterclockwise
Centisome Percentage:66.18
Left Sequence End3070694
Right Sequence End3071713
Gene Sequence:
>1020 bp
ATGACCGTACGCGTAGCGATAAATGGCTTCGGTCGCATCGGGCGTAATGTGGTTCGTGCT
TTGTATGAATCCGGACGCCGGGCGGAAATTACCGTGGTGGCAATCAACGAACTGGCGGAT
GCTGCGGGCATGGCGCATTTGTTGAAATATGACACCAGCCATGGCCGTTTTGCATGGGAA
GTACGACAGGAACGCGATCAACTTTTTGTTGGTGATGACGCCATCCGCGTATTGCATGAA
CGTTCACTGCAATCGCTCCCCTGGCGTGAACTTGGCGTTGATGTAGTCCTCGACTGCACC
GGCGTATATGGCTCCCGCGAGCATGGCGAAGCGCATATTGCCGCCGGGGCCAAAAAAGTG
CTCTTTTCACATCCTGGCAGTAACGATCTCGACGCGACCGTTGTTTACGGCGTCAATCAG
GATCAACTTCGTGCGGAACACCGCATCGTTTCTAACGCTTCCTGTACCACGAATTGCATA
ATTCCCGTCATCAAATTGTTAGATGATGCGTACGGTATTGAGTCCGGCACTGTGACCACA
ATTCACTCCGCCATGCACGATCAACAGGTTATTGATGCATACCATCCTGACCTGCGTCGC
ACCCGGGCAGCCAGCCAGTCGATCATTCCGGTCGATACTAAACTGGCCGCCGGTATCACA
CGATTTTTTCCGCAATTTAACGATCGCTTTGAAGCGATTGCGGTACGTGTGCCAACCATA
AATGTGACGGCAATCGATTTAAGCGTGACGGTGAAGAAACCTGTAAAAGCCAATGAAGTC
AACCTGTTGCTGCAAAAAGCAGCACAAGGTGCATTTCATGGTATAGTTGACTATACGGAA
TTGCCGTTGGTCTCTGTAGATTTTAACCACGATCCGCACAGTGCCATTGTCGATGGCACC
CAAACCCGGGTCAGTGGCGCACACCTGATCAAAACGTTGGTCTGGTGCGATAACGAATGG
GGCTTTGCTAACCGAATGCTCGACACGACGTTAGCTATGGCTACTGTTGCTTTCAGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:339
Protein Molecular Weight:37299
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>D-erythrose-4-phosphate dehydrogenase
MTVRVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWE
VRQERDQLFVGDDAIRVLHERSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKV
LFSHPGSNDLDATVVYGVNQDQLRAEHRIVSNASCTTNCIIPVIKLLDDAYGIESGTVTT
IHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTI
NVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYTELPLVSVDFNHDPHSAIVDGT
QTRVSGAHLIKTLVWCDNEWGFANRMLDTTLAMATVAFR
References
External Links:
ResourceLink
Uniprot ID:P0A9B6
Uniprot Name:E4PD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675738
Ecogene ID:EG10368
Ecocyc:EG10368
ColiBase:b2927
Kegg Gene:b2927
EchoBASE ID:EB0363
CCDB:E4PD_ECOLI
BacMap:16130828
General Reference:
  • Alefounder, P. R., Perham, R. N. (1989). "Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli." Mol Microbiol 3:723-732. Pubmed: 2546007
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Boschi-Muller, S., Azza, S., Pollastro, D., Corbier, C., Branlant, G. (1997). "Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase." J Biol Chem 272:15106-15112. Pubmed: 9182530
  • Doolittle, R. F., Feng, D. F., Anderson, K. L., Alberro, M. R. (1990). "A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote." J Mol Evol 31:383-388. Pubmed: 2124629
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Yang, Y., Zhao, G., Man, T. K., Winkler, M. E. (1998). "Involvement of the gapA- and epd (gapB)-encoded dehydrogenases in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12." J Bacteriol 180:4294-4299. Pubmed: 9696782
  • Zhao, G., Pease, A. J., Bharani, N., Winkler, M. E. (1995). "Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis." J Bacteriol 177:2804-2812. Pubmed: 7751290