Erythronate-4-phosphate dehydrogenase (P05459)

Identification
Name:Erythronate-4-phosphate dehydrogenase
Synonyms:Not Available
Gene Name:pdxB
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific Function:Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Phospho-D-erythronate + 1.0NAD ↔ 1.0Hydrogen ion + 1.0NADH + 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Phospho-D-erythronate + 1.0NAD ↔ 1.0Hydrogen ion + 1.0NADH + 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Phospho-D-erythronate + 1.0NAD → 1.0Hydrogen ion + 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid + 1.0NADH
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.04-Phospho-D-erythronate + 1.0NAD → 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB068012-Oxo-3-hydroxy-4-phosphobutanoic acidMetaboCard
ECMDB200954-Phospho-D-erythronateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
4-phosphoerythronate dehydrogenase activity
binding
catalytic activity
cofactor binding
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
metabolic process
pyridoxine biosynthetic process
pyridoxine metabolic process
small molecule metabolic process
vitamin B6 metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Properties
Blattner:b2320
Gene OrientationCounterclockwise
Centisome Percentage:52.48
Left Sequence End2434737
Right Sequence End2435873
Gene Sequence:
>1137 bp
ATGTTTGATTATGAAACATTGCGCTTCATCTGGTGGCTGCTGATTGGCGTGATCCTGGTG
GTCTTTATGATCTCCGACGGATTTGACATGGGGATCGGCTGTCTGCTGCCGCTGGTGGCG
CGTAATGATGATGAACGCCGGATAGTGATAAACAGCGTTGGTGCACACTGGGAAGGCAAC
CAGGTCTGGTTGATCCTCGCTGGTGGGGCATTATTTGCCGCCTGGCCCAGAGTGTATGCA
GCGGCGTTTTCCGGCTTTTATGTGGCGATGATCCTGGTGCTGTGCTCACTGTTCTTCCGC
CCGCTGGCCTTTGATTATCGCGGAAAAATCGCCGATGCACGCTGGCGTAAAATGTGGGAC
GCCGGTCTGGTCATCGGCAGTCTGGTGCCGCCGGTAGTCTTCGGTATCGCCTTCGGCAAC
TTGTTGCTCGGCGTGCCGTTTGCCTTCACACCGCAATTACGCGTGGAGTATCTCGGCAGC
TTCTGGCAACTGCTGACGCCATTCCCTTTATTGTGCGGATTGCTCAGCCTTGGGATGGTG
ATTTTGCAAGGTGGCGTCTGGTTACAACTGAAAACTGTTGGTGTGATTCATCTGCGTTCA
CAGCTGGCGACCAAACGCGCTGCACTGTTGGTGATGCTGTGCTTTTTGCTGGCGGGTTAC
TGGCTGTGGGTCGGTATTGATGGCTTTGTACTGCTCGCCCAGGATGCTAACGGTCCTTCC
AATCCGTTAATGAAACTGGTGGCAGTGCTACCTGGTGCCTGGATGAATAATTTTGTCGAG
TCGCCCGTTTTGTGGATCTTCCCGCTGCTGGGATTCTTCTGCCCATTGCTGACGGTGATG
GCGATTTATCGTGGTCGCCCGGGTTGGGGATTTTTGATGGCATCATTGATGCAATTTGGC
GTGATTTTCACGGCAGGCATCACGCTGTTCCCCTTTGTCATGCCGTCAAGCGTGAGTCCG
ATCTCCAGCCTGACGTTGTGGGACAGTACTTCCAGTCAGCTGACGCTGAGCATTATGTTG
GTAATCGTGCTGATATTTTTGCCCATTGTGTTGCTCTACACTCTCTGGAGCTACTACAAA
ATGTGGGGGCGCATGACAACAGAAACTCTCCGCCGTAACGAAAACGAGTTGTACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:378
Protein Molecular Weight:41367
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Erythronate-4-phosphate dehydrogenase
MKILVDENMPYARDLFSRLGEVTAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIK
FVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLYDRTVG
IVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEGDFRSLDELVQRADILTFHTPLFKD
GPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPEL
NVELLKKVDIGTSHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITL
HGPLDQPTLKRLVHLVYDVRRDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDAS
AASLLCKLGFNAVHHPAR
References
External Links:
ResourceLink
Uniprot ID:P05459
Uniprot Name:PDXB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651480
Ecogene ID:EG10692
Ecocyc:EG10692
ColiBase:b2320
Kegg Gene:b2320
EchoBASE ID:EB0686
CCDB:PDXB_ECOLI
BacMap:16130255
General Reference:
  • Arps, P. J., Marvel, C. C., Rubin, B. C., Tolan, D. A., Penhoet, E. E., Winkler, M. E. (1985). "Structural features of the hisT operon of Escherichia coli K-12." Nucleic Acids Res 13:5297-5315. Pubmed: 2991861
  • Arps, P. J., Winkler, M. E. (1987). "Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette." J Bacteriol 169:1061-1070. Pubmed: 3029016
  • 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
  • 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
  • Pease, A. J., Roa, B. R., Luo, W., Winkler, M. E. (2002). "Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12." J Bacteriol 184:1359-1369. Pubmed: 11844765
  • Schoenlein, P. V., Roa, B. B., Winkler, M. E. (1989). "Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12." J Bacteriol 171:6084-6092. Pubmed: 2681152
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • 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., Winkler, M. E. (1996). "4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12." FEMS Microbiol Lett 135:275-280. Pubmed: 8595869