4-hydroxythreonine-4-phosphate dehydrogenase (P19624)

Identification
Name:4-hydroxythreonine-4-phosphate dehydrogenase
Synonyms:
  • 4-(phosphohydroxy)-L-threonine dehydrogenase
Gene Name:pdxA
Enzyme Class:
Biological Properties
General Function:Involved in 4-hydroxythreonine-4-phosphate dehydrogenase activity
Specific Function:Catalyzes the NAD(P)-dependent oxidation of 4- (phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4- (phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP)
Cellular Location:Cytoplasm
SMPDB Pathways:
  • Operon: 16S ribosomal RNA modification & chaperone PW001877
  • Vitamin B6 1430936196 PW000891
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0O-Phospho-4-hydroxy-L-threonine + 1.0NAD ↔ 1.02-Amino-3-oxo-4-phosphonooxybutyrate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0NAD + 1.02-Amino-3-oxo-4-phosphonooxybutyrate + 1.0O-Phospho-4-hydroxy-L-threonine ↔ 1.03-Amino-2-oxopropyl phosphate + 1.0Carbon dioxide + 1.0NADH + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0O-Phospho-4-hydroxy-L-threonine + 1.0NAD ↔ 1.02-Amino-3-oxo-4-phosphonooxybutyrate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.01-Deoxy-D-xylulose 5-phosphate + 1.0NAD + 1.0O-Phospho-4-hydroxy-L-threonine → 1.0Carbon dioxide + 1.0Hydrogen ion + 2.0Water + 1.0NADH + 1.0Pyridoxine 5'-phosphate + 1.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB040141-Amino-propan-2-one-3-phosphateMetaboCard
ECMDB012131-Deoxy-D-xylulose 5-phosphateMetaboCard
ECMDB200362-Amino-3-oxo-4-phosphonooxybutyrateMetaboCard
ECMDB237753-Amino-2-oxopropyl phosphateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB06802O-Phospho-4-hydroxy-L-threonineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB01319Pyridoxine 5'-phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
4-hydroxythreonine-4-phosphate dehydrogenase activity
binding
catalytic activity
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
oxidation reduction
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:b0052
Gene OrientationCounterclockwise
Centisome Percentage:1.13
Left Sequence End52427
Right Sequence End53416
Gene Sequence:
>990 bp
ATGGTTAAAACCCAACGTGTTGTGATCACTCCCGGCGAGCCCGCCGGGATTGGCCCGGAC
TTAGTTGTCCAGCTTGCACAGCGTGAGTGGCCGGTCGAACTGGTTGTTTGTGCCGATGCC
ACTCTCCTTACCAACCGGGCAGCGATGCTCGGTTTGCCGCTCACCCTCCGCCCTTATTCC
CCCAACTCCCCTGCACAACCGCAAACTGCGGGCACATTAACGCTACTTCCTGTCGCGCTA
CGTGCACCTGTCACTGCGGGGCAGTTAGCGGTTGAAAATGGGCATTATGTGGTGGAAACG
CTGGCGCGAGCGTGCGATGGTTGTCTGAACGGCGAATTTGCCGCGCTGATCACAGGTCCG
GTGCATAAAGGCGTTATTAACGACGCTGGCATTCCTTTTACCGGTCATACCGAGTTTTTC
GAAGAGCGTTCGCAGGCGAAAAAGGTGGTGATGATGCTGGCGACCGAAGAACTTCGCGTG
GCGCTGGCAACGACGCATTTACCGCTGCGCGATATCGCAGACGCTATCACCCCTGCACTT
TTGCACGAAGTGATTGCTATTTTGCATCACGATTTGCGGACCAAATTTGGTATTGCCGAA
CCGCGCATTCTGGTCTGCGGGCTGAATCCGCACGCGGGCGAAGGCGGTCATATGGGTACG
GAAGAGATAGACACCATTATTCCGGTGCTCAATGAGCTGCGGGCGCAGGGGATGAAACTC
AACGGGCCGCTGCCTGCCGATACCCTGTTTCAGCCGAAATATCTTGATAACGCCGACGCC
GTGCTGGCGATGTACCACGATCAGGGTCTTCCCGTGCTAAAATACCAGGGCTTCGGGCGC
GGTGTGAACATTACGCTGGGCCTGCCCTTTATTCGCACATCAGTGGACCACGGCACCGCG
CTTGAACTGGCGGGACGTGGCAAAGCCGATGTCGGCAGTTTTATTACGGCGCTTAATCTC
GCCATCAAAATGATTGTTAACACCCAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:329
Protein Molecular Weight:35114
Protein Theoretical pI:6
PDB File:1PS6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>4-hydroxythreonine-4-phosphate dehydrogenase
MVKTQRVVITPGEPAGIGPDLVVQLAQREWPVELVVCADATLLTNRAAMLGLPLTLRPYS
PNSPAQPQTAGTLTLLPVALRAPVTAGQLAVENGHYVVETLARACDGCLNGEFAALITGP
VHKGVINDAGIPFTGHTEFFEERSQAKKVVMMLATEELRVALATTHLPLRDIADAITPAL
LHEVIAILHHDLRTKFGIAEPRILVCGLNPHAGEGGHMGTEEIDTIIPVLNELRAQGMKL
NGPLPADTLFQPKYLDNADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTA
LELAGRGKADVGSFITALNLAIKMIVNTQ
References
External Links:
ResourceLink
Uniprot ID:P19624
Uniprot Name:PDXA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321932
PDB ID:1PS6
Ecogene ID:EG10691
Ecocyc:EG10691
ColiBase:b0052
Kegg Gene:b0052
EchoBASE ID:EB0685
CCDB:PDXA_ECOLI
BacMap:16128046
General Reference:
  • Banks, J., Cane, D. E. (2004). "Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-l-threonine-4-phosphate using electrospray ionization mass spectrometry." Bioorg Med Chem Lett 14:1633-1636. Pubmed: 15026039
  • 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
  • Roa, B. B., Connolly, D. M., Winkler, M. E. (1989). "Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12." J Bacteriol 171:4767-4777. Pubmed: 2670894
  • Sivaraman, J., Li, Y., Banks, J., Cane, D. E., Matte, A., Cygler, M. (2003). "Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway." J Biol Chem 278:43682-43690. Pubmed: 12896974
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901