Dihydroneopterin aldolase (P0AC16)

Identification
Name:Dihydroneopterin aldolase
Synonyms:
  • DHNA
Gene Name:folB
Enzyme Class:
Biological Properties
General Function:Involved in dihydroneopterin aldolase activity
Specific Function:Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin at appreciable velocity
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.07,8-Dihydroneopterin ↔ 1.06-Hydroxymethyl dihydropterin + 1.0Glycolaldehyde
ReactionCard
SMPDB Reactions:
1.07,8-Dihydroneopterin+1.0Thumb → 1.0Thumb+1.0Thumb
1.07,8-Dihydroneopterin + 1.07,8-Dihydroneopterin → 1.0Glycolaldehyde + 1.06-Hydroxymethyl dihydropterin
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.07,8-Dihydroneopterin ↔ 1.06-Hydroxymethyl dihydropterin + 1.0Glycolaldehyde
ReactionCard
1.0Thumb ↔ 1.0Thumb
1.07,8-Dihydroneopterin ↔ 1.07,8-Dihydroneopterin
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB214852-Amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridineMetaboCard
ECMDB211816-Hydroxymethyl dihydropterinMetaboCard
ECMDB022757,8-DihydroneopterinMetaboCard
ECMDB02165GlycolaldehydeMetaboCard
GO Classification:
Function
aldehyde-lyase activity
carbon-carbon lyase activity
catalytic activity
dihydroneopterin aldolase activity
lyase activity
Process
cellular aromatic compound metabolic process
cellular metabolic process
folic acid and derivative metabolic process
metabolic process
Gene Properties
Blattner:b3058
Gene OrientationCounterclockwise
Centisome Percentage:69.02
Left Sequence End3202243
Right Sequence End3202611
Gene Sequence:
>369 bp
ATGAAATATAGTTCAATATTTTCGATGCTTTCATTTTTTATACTATTTGCCTGTAATGAG
ACAGCTGTTTACGGTTCTGATGAAAACATTATTTTTATGAGGTATGTGGAAAAATTACAT
TTAGATAAATACTCTGTTAAAAATACGGTAAAAACTGAAACAATGGCGATACAATTAGCT
GAAATATATGTTAGGTATCGCTATGGCGAACGGATTGCAGAAGAAGAAAAACCATATTTA
ATTACGGAACTACCAGATAGTTGGGTTGTTGAGGGAGCAAAGTTACCTTATGAAGTTGCG
GGTGGTGTATTTATTATAGAAATTAATAAGAAAAATGGATGTGTTTTGAATTTCCTACAT
AGTAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:122
Protein Molecular Weight:13619
Protein Theoretical pI:4
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Dihydroneopterin aldolase
MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETV
VSHVEGARFALVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLKE
NN
References
External Links:
ResourceLink
Uniprot ID:P0AC16
Uniprot Name:FOLB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674637
Ecogene ID:EG11673
Ecocyc:EG11673
ColiBase:b3058
Kegg Gene:b3058
EchoBASE ID:EB1624
CCDB:FOLB_ECOLI
BacMap:90111533
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
  • Cain, B. D., Norton, P. J., Eubanks, W., Nick, H. S., Allen, C. M. (1993). "Amplification of the bacA gene confers bacitracin resistance to Escherichia coli." J Bacteriol 175:3784-3789. Pubmed: 8389741
  • Haussmann, C., Rohdich, F., Schmidt, E., Bacher, A., Richter, G. (1998). "Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase." J Biol Chem 273:17418-17424. Pubmed: 9651328
  • 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