L-fuculose phosphate aldolase
Details
- Name
- L-fuculose phosphate aldolase
- Synonyms
- 4.1.2.17
- fucC
- L-fuculose-1-phosphate aldolase
- prd
- Gene Name
- fucA
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011467|L-fuculose phosphate aldolase MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDG NGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGG NSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQL YLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE
- Number of residues
- 215
- Molecular Weight
- 23775.11
- Theoretical pI
- 6.58
- GO Classification
- Functionsaldehyde-lyase activity / L-fuculose-phosphate aldolase activity / zinc ion bindingProcessesD-arabinose catabolic process / L-fucose catabolic process
- General Function
- Zinc ion binding
- Specific Function
- Catalyzes the cleavage of L-fuculose 1-phosphate to glycerone phosphate and L-lactaldehyde.
- Pfam Domain Function
- Aldolase_II (PF00596)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011468|L-fuculose phosphate aldolase (fucA) ATGGAACGAAATAAACTTGCTCGTCAGATTATTGACACTTGCCTGGAAATGACCCGCCTG GGACTGAACCAGGGGACAGCGGGGAACGTCAGTGTACGTTATCAGGATGGGATGCTGATT ACGCCTACAGGCATTCCATATGAAAAACTGACGGAGTCGCATATTGTCTTTATTGATGGC AACGGTAAACATGAGGAAGGAAAGCTCCCCTCAAGCGAATGGCGTTTCCATATGGCAGCC TATCAAAGCAGACCGGATGCCAACGCGGTTGTTCACAATCATGCCGTTCATTGCACGGCA GTTTCCATTCTTAACCGATCGATCCCCGCTATTCACTACATGATTGCGGCGGCTGGCGGT AATTCTATTCCTTGCGCGCCTTATGCGACCTTTGGAACACGCGAACTTTCTGAACATGTT GCGCTGGCTCTCAAAAATCGTAAGGCAACTTTGTTACAACATCATGGGCTTATCGCTTGT GAGGTGAATCTGGAAAAAGCGTTATGGCTGGCGCATGAAGTTGAAGTGCTGGCGCAACTT TACCTGACGACCCTGGCGATTACGGACCCGGTGCCAGTGCTGAGCGATGAAGAGATTGCC GTAGTGCTGGAGAAATTCAAAACCTATGGGTTACGAATTGAAGAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0AB87 UniProtKB Entry Name FUCA_ECOLI GenBank Protein ID 7144488 GenBank Gene ID M31059 - General References
- Lu Z, Lin EC: The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation. Nucleic Acids Res. 1989 Jun 26;17(12):4883-4. [Article]
- Chen YM, Lu Z, Lin EC: 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. 1989 Nov;171(11):6097-105. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Conway T, Ingram LO: Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae. J Bacteriol. 1989 Jul;171(7):3754-9. [Article]
- GHALAMBOR MA, HEATH EC: The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-phosphate. J Biol Chem. 1962 Aug;237:2427-33. [Article]
- Dreyer MK, Schulz GE: The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli. J Mol Biol. 1993 Jun 5;231(3):549-53. [Article]
- Dreyer MK, Schulz GE: Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J Mol Biol. 1996 Jun 14;259(3):458-66. [Article]
- Dreyer MK, Schulz GE: Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. [Article]
- Joerger AC, Gosse C, Fessner WD, Schulz GE: Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis. Biochemistry. 2000 May 23;39(20):6033-41. [Article]
- Joerger AC, Mueller-Dieckmann C, Schulz GE: Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis. J Mol Biol. 2000 Nov 3;303(4):531-43. [Article]