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Sequence of FUCA_ECOLI

EC Number:4.1.2.17

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
L-fuculose-phosphate aldolase
P0AB87
Escherichia coli (strain K12)
215
23775
Reaction
L-Fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Other sequences found for EC No. 4.1.2.17

General information:

Sequence
show sequence in fasta format
  0 MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG
 60 NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRSIPA IHYMIAAAGG
120 NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EVNLEKALWL AHEVEVLAQL
180 YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1176717
Lu Z.,Lin E.C.C.
The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation.
Nucleic Acids Res.
17
4883-4884
1989
1176718
Chen Y.M.,Lu Z.,Lin E.C.C.
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
1989
1176719
Blattner F.R.,Plunkett G. III,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.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
1176720
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
1176721
Conway T.,Ingram L.O.
Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae.
J. Bacteriol.
171
3754-3759
1989
1176722
Ghalambor M.A.,Heath E.C.
The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate.
J. Biol. Chem.
237
2427-2433
1962
1176723
LeBlanc D.J.,Mortlock R.P.
Metabolism of D-arabinose: a new pathway in Escherichia coli.
J. Bacteriol.
106
90-96
1971
1176726
Dreyer M.K.,Schulz G.E.
The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
J. Mol. Biol.
231
549-553
1993
1176727
Dreyer M.K.,Schulz G.E.
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
Acta Crystallogr. D
52
1082-1091
1996
1176728
Dreyer M.K.,Schulz G.E.
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
J. Mol. Biol.
259
458-466
1996
1176729
Joerger A.C.,Gosse C.,Fessner W.-D.,Schulz G.E.
Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.
Biochemistry
39
6033-6041
2000
1176730
Joerger A.C.,Mueller-Dieckmann C.,Schulz G.E.
Structures of L-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.
J. Mol. Biol.
303
531-543
2000