L-fuculose phosphate aldolase (P0AB87)

Identification
Name:L-fuculose phosphate aldolase
Synonyms:
  • L-fuculose-1-phosphate aldolase
Gene Name:fucA
Enzyme Class:
Biological Properties
General Function:Involved in metal ion binding
Specific Function:L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Fructose and mannose metabolism ec00051
  • Microbial metabolism in diverse environments ec01120
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Fuculose 1-phosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde + 1.0(S)-Lactaldehyde
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Fuculose 1-phosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde
ReactionCard
SMPDB Reactions:
1.0L-fuculose 1-phosphate+1.0Thumb → 1.0Thumb+1.0(S)-lactaldehyde+1.0Thumb
1.0L-fuculose 1-phosphate + 1.0L-Fuculose 1-phosphate → 1.0Dihydroxyacetone phosphate + 1.0(S)-lactaldehyde + 1.0Lactaldehyde
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Glycerone phosphate
1.0D-Ribulose-1-phosphate ↔ 1.0Glycolaldehyde + 1.0Glycerone phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Fuculose 1-phosphate ↔ 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde + 1.0(S)-Lactaldehyde
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Fuculose 1-phosphate → 1.0Dihydroxyacetone phosphate + 1.0Lactaldehyde
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB23841(S)-LactaldehydeMetaboCard
ECMDB20544D-Ribulose-1-phosphateMetaboCard
ECMDB01473Dihydroxyacetone phosphateMetaboCard
ECMDB02165GlycolaldehydeMetaboCard
ECMDB20165L-Fuculose 1-phosphateMetaboCard
ECMDB03052LactaldehydeMetaboCard
GO Classification:
Function
aldehyde-lyase activity
binding
carbon-carbon lyase activity
catalytic activity
cation binding
ion binding
L-fuculose-phosphate aldolase activity
lyase activity
metal ion binding
transition metal ion binding
zinc ion binding
Process
alcohol metabolic process
fucose metabolic process
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b2800
Gene OrientationCounterclockwise
Centisome Percentage:63.17
Left Sequence End2931063
Right Sequence End2931710
Gene Sequence:
>648 bp
ATGGCACGAAAAACCAAACAAGAAGCGCAAGAAACGCGCCAACACATCCTCGATGTGGCT
CTACGTCTTTTCTCACAGCAGGGGGTATCATCCACCTCGCTGGGCGAGATTGCAAAAGCA
GCTGGCGTTACGCGCGGTGCAATCTACTGGCATTTTAAAGACAAGTCGGATTTGTTCAGT
GAGATCTGGGAACTGTCAGAATCCAATATTGGTGAACTAGAGCTTGAGTATCAGGCAAAA
TTCCCTGGCGATCCACTCTCAGTATTAAGAGAGATATTAATTCATGTTCTTGAATCCACG
GTGACAGAAGAACGGCGTCGATTATTGATGGAGATTATATTCCACAAATGCGAATTTGTC
GGAGAAATGGCTGTTGTGCAACAGGCACAACGTAATCTCTGTCTGGAAAGTTATGACCGT
ATAGAACAAACGTTAAAACATTGTATTGAAGCGAAAATGTTGCCTGCGGATTTAATGACG
CGTCGCGCAGCAATTATTATGCGCGGCTATATTTCCGGCCTGATGGAAAACTGGCTCTTT
GCCCCGCAATCTTTTGATCTTAAAAAAGAAGCCCGCGATTACGTTGCCATCTTACTGGAG
ATGTATCTCCTGTGCCCCACGCTTCGTAATCCTGCCACTAACGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:215
Protein Molecular Weight:23775
Protein Theoretical pI:7
PDB File:4FUA
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>L-fuculose phosphate aldolase
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDG
NGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGG
NSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQL
YLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE
References
External Links:
ResourceLink
Uniprot ID:P0AB87
Uniprot Name:FUCA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674603
PDB ID:4FUA
Ecogene ID:EG10348
Ecocyc:EG10348
ColiBase:b2800
Kegg Gene:b2800
EchoBASE ID:EB0344
CCDB:FUCA_ECOLI
BacMap:16130707
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
  • Chen, Y. M., Lu, Z., Lin, E. C. (1989). "Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol." J Bacteriol 171:6097-6105. Pubmed: 2553671
  • Conway, T., Ingram, L. O. (1989). "Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae." J Bacteriol 171:3754-3759. Pubmed: 2661535
  • Dreyer, M. K., Schulz, G. E. (1993). "The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli." J Mol Biol 231:549-553. Pubmed: 8515438
  • Dreyer, M. K., Schulz, G. E. (1996). "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure." J Mol Biol 259:458-466. Pubmed: 8676381
  • Dreyer, M. K., Schulz, G. E. (1996). "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli." Acta Crystallogr D Biol Crystallogr 52:1082-1091. Pubmed: 15299567
  • 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
  • Joerger, A. C., Gosse, C., Fessner, W. D., Schulz, G. E. (2000). "Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis." Biochemistry 39:6033-6041. Pubmed: 10821675
  • Joerger, A. C., Mueller-Dieckmann, C., Schulz, G. E. (2000). "Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis." J Mol Biol 303:531-543. Pubmed: 11054289
  • Lu, Z., Lin, E. C. (1989). "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation." Nucleic Acids Res 17:4883-4884. Pubmed: 2664711