PUL ID

PUL0245

PubMed

24333485, J Mol Biol. 2014 Apr 3;426(7):1469-82. doi: 10.1016/j.jmb.2013.12.006. Epub 2013 Dec 12.

Characterization method

enzyme activity assay, gene deletion mutant and growth assay, Western Blot

Genomic accession number

AE005672.3

Nucelotide position range

2072292-2085657

Substrate

fucose

Loci

SP_2158-SP_2168

Species

Streptococcus pneumoniae/1313

Degradation or Biosynthesis

degradation

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

fucI 1 - 1767 (-) CDS No
- 1850 - 4966 (-) CAZyme: GH98|CBM47 Yes
- 4976 - 7270 (-) CAZyme: GH95 Yes
- 7329 - 8129 (-) TC: gnl|TC-DB|Q97N94|4.A.6.1.9 Yes
- 8126 - 8899 (-) TC: gnl|TC-DB|Q97N93|4.A.6.1.9 Yes
- 8924 - 9394 (-) TC: gnl|TC-DB|Q97N92|4.A.6.1.9 Yes
- 9385 - 9816 (-) TC: gnl|TC-DB|Q97N91|4.A.6.1.9 Yes
fucU 9806 - 10249 (-) CDS No
fucA 10261 - 10899 (-) CDS No
- 11014 - 12417 (-) CDS No
- 12593 - 13366 (+) TF: DBD-Pfam|HTH_DeoR,DBD-SUPERFAMILY|0043758 No

PUL ID

PUL0245

PubMed

24333485, J Mol Biol. 2014 Apr 3;426(7):1469-82. doi: 10.1016/j.jmb.2013.12.006. Epub 2013 Dec 12.

Title

Structural and functional analysis of fucose-processing enzymes from Streptococcus pneumoniae.

Author

Higgins MA, Suits MD, Marsters C, Boraston AB

Abstract

Fucose metabolism pathways are present in many bacterial species and typically contain the central fucose-processing enzymes fucose isomerase (FcsI), fuculose kinase (FcsK), and fuculose-1-phosphate aldolase (FcsA). Fucose initially undergoes isomerization by FcsI producing fuculose, which is then phosphorylated by FcsK. FcsA cleaves the fuculose-1-phosphate product into lactaldehyde and dihydroxyacetone phosphate, which can be incorporated into central metabolism allowing the bacterium to use fucose as an energy source. Streptococcus pneumoniae has fucose-processing operons containing homologs of FcsI, FcsK, and FcsA; however, this bacterium appears unable to utilize fucose as an energy source. To investigate this contradiction, we performed biochemical and structural studies of the S. pneumoniae fucose-processing enzymes SpFcsI, SpFcsK, and SpFcsA. These enzymes are demonstrated to act in a sequential manner to ultimately produce dihydroxyacetone phosphate and have structural features entirely consistent with their observed biochemical activities. Analogous to the regulation of the Escherichia coli fucose utilization operon, fuculose-1-phosphate appears to act as an inducing molecule for activation of the S. pneumoniae fucose operon. Despite our evidence that S. pneumoniae appears to have the appropriate regulatory and biochemical machinery for fucose metabolism, we confirmed the inability of the S. pneumoniae TIGR4 strain to grow on fucose or on the H-disaccharide, which is the probable substrate of the transporter for the pathway. On the basis of these observations, we postulate that the S. pneumoniae fucose-processing pathway has a non-metabolic role in the interaction of this bacterium with its human host.