PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL (P76014)

Identification
Name:PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL
Synonyms:Not Available
Gene Name:dhaL
Enzyme Class:Not Available
Biological Properties
General Function:Involved in glycerone kinase activity
Specific Function:ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for phosphorylating dihydroxyacetone. DhaL- ADP receives a phosphoryl group from dhaM and transmits it to dihydroxyacetone. DhaL-ADP acts also as a coactivator by binding to the sensor domain of dhaR. DhaL-ATP is inactive
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Dihydroxyacetone ↔ 1.0ADP + 1.0Dihydroxyacetone phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Dihydroxyacetone + 1.0Phosphoenolpyruvic acid → 1.0Dihydroxyacetone phosphate + 1.0Pyruvic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01882DihydroxyacetoneMetaboCard
ECMDB01473Dihydroxyacetone phosphateMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00243Pyruvic acidMetaboCard
GO Classification:
Function
catalytic activity
glycerone kinase activity
kinase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolic process
alditol metabolic process
glycerol metabolic process
metabolic process
polyol metabolic process
small molecule metabolic process
Gene Properties
Blattner:b1199
Gene OrientationCounterclockwise
Centisome Percentage:26.91
Left Sequence End1248348
Right Sequence End1248980
Gene Sequence:
>633 bp
ATGTCACTGAGCAGAACTCAAATTGTTAACTGGCTCACTCGTTGTGGCGATATTTTCAGC
ACCGAGAGCGAGTATCTTACCGGACTGGATCGCGAAATTGGCGATGCTGACCACGGGCTA
AATATGAACCGAGGCTTTAGCAAAGTGGTGGAAAAACTCCCTGCTATCGCAGATAAAGAT
ATCGGTTTCATTCTCAAGAATACCGGTATGACGCTGCTTTCCAGCGTCGGTGGTGCCAGT
GGTCCGCTGTTCGGTACCTTCTTTATCCGCGCCGCACAGGCGACCCAGGCACGGCAAAGC
CTGACACTGGAAGAGCTTTATCAGATGTTCCGCGATGGCGCGGACGGCGTAATCAGTCGC
GGGAAAGCCGAACCTGGCGATAAAACCATGTGTGATGTGTGGGTGCCGGTGGTGGAATCG
TTACGTCAGTCCAGCGAGCAAAATCTCTCTGTTCCGGTGGCGCTCGAAGCTGCCAGTAGC
ATCGCCGAATCCGCTGCACAAAGTACGATTACGATGCAAGCCCGCAAAGGCCGCGCCAGT
TATCTCGGTGAACGCAGTATTGGTCACCAGGATCCCGGCGCGACCTCGGTGATGTTTATG
ATGCAAATGTTGGCGTTAGCCGCAAAAGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:210
Protein Molecular Weight:22632
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>PTS-dependent dihydroxyacetone kinase, ADP-binding subunit dhaL
MSLSRTQIVNWLTRCGDIFSTESEYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKD
IGFILKNTGMTLLSSVGGASGPLFGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISR
GKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPVALEAASSIAESAAQSTITMQARKGRAS
YLGERSIGHQDPGATSVMFMMQMLALAAKE
References
External Links:
ResourceLink
Uniprot ID:P76014
Uniprot Name:DHAL_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674873
Ecogene ID:EG13900
Ecocyc:EG13900
ColiBase:b1199
Kegg Gene:b1199
EchoBASE ID:EB3659
CCDB:DHAL_ECOLI
BacMap:16129162
General Reference:
  • Bachler, C., Flukiger-Bruhwiler, K., Schneider, P., Bahler, P., Erni, B. (2005). "From ATP as substrate to ADP as coenzyme: functional evolution of the nucleotide binding subunit of dihydroxyacetone kinases." J Biol Chem 280:18321-18325. Pubmed: 15753087
  • 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
  • Fountoulakis, M., Takacs, M. F., Berndt, P., Langen, H., Takacs, B. (1999). "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Electrophoresis 20:2181-2195. Pubmed: 10493123
  • Gutknecht, R., Beutler, R., Garcia-Alles, L. F., Baumann, U., Erni, B. (2001). "The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor." EMBO J 20:2480-2486. Pubmed: 11350937
  • 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
  • Oberholzer, A. E., Schneider, P., Baumann, U., Erni, B. (2006). "Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase." J Mol Biol 359:539-545. Pubmed: 16647083
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232