Aldolases of the DhnA family: a possible solution to the problem of pentose and hexose biosynthesis in archaea.
Sequence analysis of the recently identified class I aldolase of Escherichia coli (dhnA gene product) helped to identify its homologs in Chlamydia trachomatis, Chlamydiophyla pneumoniae and in each of the completely sequenced archaeal genomes. Iterative database searches revealed sequence similarities between the DhnA-family enzymes, deoxyribose phosphate aldolases and bacterial (class II) fructose bisphosphate aldolases and allowed prediction of similar three-dimensional structures (TIM-barrel fold) in all these enzymes. The Schiff base-forming lysyl residues of DhnA and deoxyribose phosphate aldolase are conserved in all members of the DhnA and deoxyribose phosphate aldolase families, indicating that these enzymes share common features with both class I and class II aldolases. The DhnA-family enzymes are predicted to possess an aldolase activity and to play a critical role in sugar biosynthesis in archaea.
Galperin
M Y
MY
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA. galperin@ncbi.nlm.nih.gov
Aravind
L
L
Koonin
E V
EV
D000595:Amino Acid Sequence; D001105:Archaea / Q000378:metabolism*; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry / Q000378:metabolism*; D006601:Hexoses / Q000096:biosynthesis*; D008969:Molecular Sequence Data; D010429:Pentoses / Q000096:biosynthesis*; D017510:Protein Folding
D006601:Hexoses; D010429:Pentoses; D005634:Fructose-Bisphosphate Aldolase