4-hydroxythreonine-4-phosphate dehydrogenase

Details

Name
4-hydroxythreonine-4-phosphate dehydrogenase
Synonyms
  • 1.1.1.262
  • 4-(phosphohydroxy)-L-threonine dehydrogenase
Gene Name
pdxA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019137|4-hydroxythreonine-4-phosphate dehydrogenase
MVKTQRVVITPGEPAGIGPDLVVQLAQREWPVELVVCADATLLTNRAAMLGLPLTLRPYS
PNSPAQPQTAGTLTLLPVALRAPVTAGQLAVENGHYVVETLARACDGCLNGEFAALITGP
VHKGVINDAGIPFTGHTEFFEERSQAKKVVMMLATEELRVALATTHLPLRDIADAITPAL
LHEVIAILHHDLRTKFGIAEPRILVCGLNPHAGEGGHMGTEEIDTIIPVLNELRAQGMKL
NGPLPADTLFQPKYLDNADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTA
LELAGRGKADVGSFITALNLAIKMIVNTQ
Number of residues
329
Molecular Weight
35113.47
Theoretical pI
6.28
GO Classification
Functions
4-hydroxythreonine-4-phosphate dehydrogenase activity / cobalt ion binding / identical protein binding / magnesium ion binding / NAD binding / zinc ion binding
Processes
pyridoxal phosphate biosynthetic process / pyridoxine biosynthetic process
Components
cytoplasm
General Function
Zinc ion binding
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).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019138|4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
ATGGTTAAAACCCAACGTGTTGTGATCACTCCCGGCGAGCCCGCCGGGATTGGCCCGGAC
TTAGTTGTCCAGCTTGCACAGCGTGAGTGGCCGGTCGAACTGGTTGTTTGTGCCGATGCC
ACTCTCCTTACCAACCGGGCAGCGATGCTCGGTTTGCCGCTCACCCTCCGCCCTTATTCC
CCCAACTCCCCTGCACAACCGCAAACTGCGGGCACATTAACGCTACTTCCTGTCGCGCTA
CGTGCACCTGTCACTGCGGGGCAGTTAGCGGTTGAAAATGGGCATTATGTGGTGGAAACG
CTGGCGCGAGCGTGCGATGGTTGTCTGAACGGCGAATTTGCCGCGCTGATCACAGGTCCG
GTGCATAAAGGCGTTATTAACGACGCTGGCATTCCTTTTACCGGTCATACCGAGTTTTTC
GAAGAGCGTTCGCAGGCGAAAAAGGTGGTGATGATGCTGGCGACCGAAGAACTTCGCGTG
GCGCTGGCAACGACGCATTTACCGCTGCGCGATATCGCAGACGCTATCACCCCTGCACTT
TTGCACGAAGTGATTGCTATTTTGCATCACGATTTGCGGACCAAATTTGGTATTGCCGAA
CCGCGCATTCTGGTCTGCGGGCTGAATCCGCACGCGGGCGAAGGCGGTCATATGGGTACG
GAAGAGATAGACACCATTATTCCGGTGCTCAATGAGCTGCGGGCGCAGGGGATGAAACTC
AACGGGCCGCTGCCTGCCGATACCCTGTTTCAGCCGAAATATCTTGATAACGCCGACGCC
GTGCTGGCGATGTACCACGATCAGGGTCTTCCCGTGCTAAAATACCAGGGCTTCGGGCGC
GGTGTGAACATTACGCTGGGCCTGCCCTTTATTCGCACATCAGTGGACCACGGCACCGCG
CTTGAACTGGCGGGACGTGGCAAAGCCGATGTCGGCAGTTTTATTACGGCGCTTAATCTC
GCCATCAAAATGATTGTTAACACCCAATGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP19624
UniProtKB Entry NamePDXA_ECOLI
GenBank Protein ID147119
GenBank Gene IDM68521
General References
  1. Roa BB, Connolly DM, Winkler ME: Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12. J Bacteriol. 1989 Sep;171(9):4767-77. [Article]
  2. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Banks J, Cane DE: 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. 2004 Apr 5;14(7):1633-6. [Article]
  6. Sivaraman J, Li Y, Banks J, Cane DE, Matte A, Cygler M: Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway. J Biol Chem. 2003 Oct 31;278(44):43682-90. Epub 2003 Aug 1. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB026094-Hydroxy-L-Threonine-5-MonophosphateexperimentalunknownDetails