dbCAN-PUL

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	recombinant protein expression,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.

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