2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (P26281)

Identification
Name:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
Synonyms:
  • 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
  • PPPK
  • 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
  • HPPK
Gene Name:folK
Enzyme Class:
Biological Properties
General Function:Involved in 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
Specific Function:ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8- dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6- yl)methyl diphosphate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.06-Hydroxymethyl dihydropterin + 1.0Adenosine triphosphate → 1.06-Hydroxymethyl-dihydropterin pyrophosphate + 1.0Adenosine monophosphate + 1.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211816-Hydroxymethyl dihydropterinMetaboCard
ECMDB211826-Hydroxymethyl-dihydropterin pyrophosphateMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Function
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
catalytic activity
diphosphotransferase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
cellular aromatic compound metabolic process
cellular metabolic process
folic acid and derivative biosynthetic process
folic acid and derivative metabolic process
metabolic process
Gene Properties
Blattner:b0142
Gene OrientationCounterclockwise
Centisome Percentage:3.39
Left Sequence End157253
Right Sequence End157732
Gene Sequence:
>480 bp
ATGATCAGTCTGATTGCGGCGTTAGCGGTAGATCGCGTTATCGGCATGGAAAACGCCATG
CCGTGGAACCTGCCTGCCGATCTCGCCTGGTTTAAACGCAACACCTTAAATAAACCCGTG
ATTATGGGCCGCCATACCTGGGAATCAATCGGTCGTCCGTTGCCAGGACGCAAAAATATT
ATCCTCAGCAGTCAACCGGGTACGGACGATCGCGTAACGTGGGTGAAGTCGGTGGATGAA
GCCATCGCGGCGTGTGGTGACGTACCAGAAATCATGGTGATTGGCGGCGGTCGCGTTTAT
GAACAGTTCTTGCCAAAAGCGCAAAAACTGTATCTGACGCATATCGACGCAGAAGTGGAA
GGCGACACCCATTTCCCGGATTACGAGCCGGATGACTGGGAATCGGTATTCAGCGAATTC
CACGATGCTGATGCGCAGAACTCTCACAGCTATTGCTTTGAGATTCTGGAGCGGCGGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:159
Protein Molecular Weight:18079
Protein Theoretical pI:5
PDB File:1RB0
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVA
LETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMK
NRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW
References
External Links:
ResourceLink
Uniprot ID:P26281
Uniprot Name:HPPK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321929
PDB ID:1RB0
Ecogene ID:EG11374
Ecocyc:EG11374
ColiBase:b0142
Kegg Gene:b0142
EchoBASE ID:EB1348
CCDB:HPPK_ECOLI
BacMap:16128135
General Reference:
  • 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
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • 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
  • Liu, J. D., Parkinson, J. S. (1989). "Genetics and sequence analysis of the pcnB locus, an Escherichia coli gene involved in plasmid copy number control." J Bacteriol 171:1254-1261. Pubmed: 2537812
  • Stammers, D. K., Achari, A., Somers, D. O., Bryant, P. K., Rosemond, J., Scott, D. L., Champness, J. N. (1999). "2.0 A X-ray structure of the ternary complex of 7,8-dihydro-6-hydroxymethylpterinpyrophosphokinase from Escherichia coli with ATP and a substrate analogue." FEBS Lett 456:49-53. Pubmed: 10452528
  • Talarico, T. L., Dev, I. K., Dallas, W. S., Ferone, R., Ray, P. H. (1991). "Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100." J Bacteriol 173:7029-7032. Pubmed: 1657875
  • Talarico, T. L., Ray, P. H., Dev, I. K., Merrill, B. M., Dallas, W. S. (1992). "Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase." J Bacteriol 174:5971-5977. Pubmed: 1325970
  • Xiao, B., Shi, G., Chen, X., Yan, H., Ji, X. (1999). "Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents." Structure 7:489-496. Pubmed: 10378268