Because CGCFinder predicted no CGC for this PUL, the gene cluster depicted below contains dbCAN2 and CGC signature predictions for all genes in the PUL, instead of a predicted CGC.


PUL ID

PUL0116

PubMed

31160824, Nat Microbiol. 2019 Sep;4(9):1571-1581. doi: 10.1038/s41564-019-0466-x. Epub 2019 Jun 3.

Characterization method

expression of recombinant proteins, RNA-Seq, differential gene expression

Genomic accession number

AE015928.1

Nucelotide position range

626800-629842

Substrate

N-glycan

Loci

BT_0506-BT_0507

Species

Bacteroides thetaiotaomicron/818

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

- BT_0506 AAO75613.1 0 - 2304 (+) AE015928.1:626800-629104 -
- BT_0507 AAO75614.1 2434 - 3043 (+) AE015928.1:629234-629843 -

Cluster number

0

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 2304 (+) CAZyme: GH20 No
- 2435 - 3043 (+) STP: STP|TetR_N No

PUL ID

PUL0116

PubMed

31160824, Nat Microbiol. 2019 Sep;4(9):1571-1581. doi: 10.1038/s41564-019-0466-x. Epub 2019 Jun 3.

Title

Complex N-glycan breakdown by gut Bacteroides involves an extensive enzymatic apparatus encoded by multiple co-regulated genetic loci.

Author

Briliute J, Urbanowicz PA, Luis AS, Basle A, Paterson N, Rebello O, Hendel J, Ndeh DA, Lowe EC, Martens EC, Spencer DIR, Bolam DN, Crouch LI

Abstract

Glycans are the major carbon sources available to the human colonic microbiota. Numerous N-glycosylated proteins are found in the human gut, from both dietary and host sources, including immunoglobulins such as IgA that are secreted into the intestine at high levels. Here, we show that many mutualistic gut Bacteroides spp. have the capacity to utilize complex N-glycans (CNGs) as nutrients, including those from immunoglobulins. Detailed mechanistic studies using transcriptomic, biochemical, structural and genetic techniques reveal the pathway employed by Bacteroides thetaiotaomicron (Bt) for CNG degradation. The breakdown process involves an extensive enzymatic apparatus encoded by multiple non-adjacent loci and comprises 19 different carbohydrate-active enzymes from different families, including a CNG-specific endo-glycosidase activity. Furthermore, CNG degradation involves the activity of carbohydrate-active enzymes that have previously been implicated in the degradation of other classes of glycan. This complex and diverse apparatus provides Bt with the capacity to access the myriad different structural variants of CNGs likely to be found in the intestinal niche.