Identification
Name:Bifunctional protein hldE
Synonyms:
  • D-beta-D-heptose 7-phosphate kinase
  • D-beta-D-heptose 7-phosphotransferase
  • D-beta-D-heptose 1-phosphate adenosyltransferase
Gene Name:hldE
Enzyme Class:
Biological Properties
General Function:Involved in phosphotransferase activity, alcohol group as acceptor
Specific Function:Catalyzes the ADP transfer to D-glycero-D-manno-heptose 1-phosphate, yielding ADP-D,D-heptose
Cellular Location:Not Available
SMPDB Pathways:
  • ADP-L-glycero-Beta-D-manno-heptose biosynthesis PW002095
  • Lipopolysaccharide biosynthesis PW000831
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0Thumb+1.0D-glycero-beta-D-manno-Heptose 7-phosphate+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0D-glycero-beta-D-manno-heptose 1-phosphate+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
1.0D-glycero-beta-D-manno-heptose 1-phosphate + 1.0Adenosine triphosphate + 1.0Hydrogen ion → 1.0ADP-D-Glycero-D-manno-heptose + 1.0Pyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB20112ADP-D-Glycero-D-manno-heptoseMetaboCard
ECMDB23038D-glycero-beta-D-manno-heptose 7-phosphateMetaboCard
ECMDB21199D-Glycero-D-manno-heptose 1,7-bisphosphateMetaboCard
ECMDB21200D-Glycero-D-manno-heptose 1-phosphateMetaboCard
ECMDB21201D-Glycero-D-manno-heptose 7-phosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
catalytic activity
nucleotidyltransferase activity
phosphotransferase activity, alcohol group as acceptor
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
biosynthetic process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b3052
Gene OrientationCounterclockwise
Centisome Percentage:68.83
Left Sequence End3193342
Right Sequence End3194775
Gene Sequence:
>1434 bp
ATGTGGCCGGATAACCGTATCGCCCGTGACGCGCACTATCTTTACCGGTATGACCGTCAC
GGCAGGCTGACGGAGAAAACCGACCTCATCCCGGAAGGGGTTATCCGCACGGATGATGAG
CGCACCCACCGGTACCATTACGACAGTCAGCACCGGCTGGTGCACTACACGCGGACACAA
TATGCAGAGCCGCTGGTCGAAAGCCGCTATCTTTACGACCCGCTGGGCCGCAGGGTGGCA
AAACGGGTGTGGCGACGTGAACGGGACCTGACGGGCTGGATGTCGCTGTCACGGAAACCG
CAAGTGACCTGGTACGGCTGGGACGGCGACCGCCTGACCACGATACAGAACGACAGAACC
CGCATCCAGACGATTTATCAGCCGGGGAGCTTCACGCCACTCATCAGGGTTGAAACCGCC
ACCGGTGAGCTGGCGAAAACGCAGCGCCGCAGCCTGGCGGATACCCTTCAGCAGTCCGGC
GGCGAAGACGGTGGCAGTGTGGTGTTCCCGCCGGTGCTGGTGCAGATGCTCGACCGGCTG
GAAAGTGAAATCCTGGCTGACCGGGTGAGTGAGGAAAGCCGCCGCTGGCTGGCATCGTGC
GGCCTGACGGTGGAGCAGATGCAAAACCAGATGGACCCGGTGTACACGCCGGCGCGAAAA
ATCCACCTGTACCACTGCGACCATCGCGGCCTGCCGCTGGCGCTTGTCAGCACGGAAGGG
GCAACAGAATGGTGCGCAGAATACGATGAATGGGGCAACCTGCTGAATGAAGAGAACCCG
CATCAGCTGCAGCAGCTTATCCGCCTGCCGGGGCAGCAGTATGATGAGGAGTCCGGCCTG
TATTACAACCGCCACCGCTATTATGACCCGCTGCAGGGGAGGTATATCACTCAGGATCCG
ATTGGGCTGAAGGGGGGATGGAATTTTTATCAGTATCCGCTGAATCCGGTTCAGTATATA
GATTCAATGGGACTGGCATCAAAATATGGACACTTAAATAATGGCGGATATGGAGCGAGA
CCCAACAAACCGCCTACGCCCGATCCAAGTAAATTGCCGGACATAGCGAAACAATTAAGA
CTGCCATATCCTATTGACCAGGCCAGTAGTGCGCCTAATGTTTTCAAAACATTCTTCAGA
GCATTAAGCCCTTACGACTACACACTGTATTGCAGGAAGTGGGTAAAACCAAATCTGACT
TGTACGCCACAGGATGATTCCCAGTATCCAGGGATGGATACAAAGACAGCAAGTGATTAC
CTGCCACAGACAAATTGGCCAACAACTCAATTACCACCAGGATATACTTGTGCAGAACCC
TATTTATTCCCAGACATTAATAAACCCGATGGGCCAGCAACAGCAGGGATAGATGATTTG
GGTGAAATTTTAGCTAAGATGAAACAGAGAACATCGAGAGGAATAAGAAAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:477
Protein Molecular Weight:51050
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Bifunctional protein hldE
MKVTLPEFERAGVMVVGDVMLDRYWYGPTSRISPEAPVPVVKVNTIEERPGGAANVAMNI
ASLGANARLVGLTGIDDAARALSKSLADVNVKCDFVSVPTHPTITKLRVLSRNQQLIRLD
FEEGFEGVDPQPLHERINQALSSIGALVLSDYAKGALASVQQMIQLARKAGVPVLIDPKG
TDFERYRGATLLTPNLSEFEAVVGKCKTEEEIVERGMKLIADYELSALLVTRSEQGMSLL
QPGKAPLHMPTQAQEVYDVTGAGDTVIGVLAATLAAGNSLEEACFFANAAAGVVVGKLGT
STVSPIELENAVRGRADTGFGVMTEEELKLAVAAARKRGEKVVMTNGVFDILHAGHVSYL
ANARKLGDRLIVAVNSDASTKRLKGDSRPVNPLEQRMIVLGALEAVDWVVSFEEDTPQRL
IAGILPDLLVKGGDYKPEEIAGSKEVWANGGEVLVLNFEDGCSTTNIIKKIQQDKKG
References
External Links:
ResourceLink
Uniprot ID:P76658
Uniprot Name:HLDE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651310
Ecogene ID:EG13416
Ecocyc:EG13416
ColiBase:b3052
Kegg Gene:b3052
EchoBASE ID:EB3192
CCDB:HLDE_ECOLI
BacMap:16130948
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
  • 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
  • Kneidinger, B., Marolda, C., Graninger, M., Zamyatina, A., McArthur, F., Kosma, P., Valvano, M. A., Messner, P. (2002). "Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli." J Bacteriol 184:363-369. Pubmed: 11751812
  • McArthur, F., Andersson, C. E., Loutet, S., Mowbray, S. L., Valvano, M. A. (2005). "Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno-heptose biosynthesis." J Bacteriol 187:5292-5300. Pubmed: 16030223
  • Valvano, M. A., Marolda, C. L., Bittner, M., Glaskin-Clay, M., Simon, T. L., Klena, J. D. (2000). "The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose." J Bacteriol 182:488-497. Pubmed: 10629197
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842