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Cite: NAR/gkaa742 2020



PUL General Information

Literature Information

PUL ID

PUL0630

PubMed

33187992, Appl Environ Microbiol. 2021 Jan 15;87(3):e01714-20. doi: 10.1128/AEM.01714-20. Print 2021 Jan 15.

Characterization method

enzyme activity assay,affinity gel electrophoresis

Genomic accession number

HF548280.1

Nucelotide position range

18604-35744

Substrate

xylan

Loci

BN138_221-BN138_229

Species

termite gut metagenome/433724

Degradation or Biosynthesis

degradation

Gene Name

Locus Tag

Protein ID

Gene Position

GenBank Contig Range

EC Number

- BN138_221 CCO21033.1 0 - 3204 (+) HF548280.1:18604-21808 -
- BN138_222 CCO21034.1 3219 - 4896 (+) HF548280.1:21823-23500 -
- BN138_223 CCO21035.1 4917 - 6231 (+) HF548280.1:23521-24835 -
- BN138_224 CCO21036.1 6227 - 8558 (+) HF548280.1:24831-27162 -
- BN138_225 CCO21037.1 8714 - 11087 (+) HF548280.1:27318-29691 -
- BN138_226 CCO21038.1 11083 - 13609 (+) HF548280.1:29687-32213 -
- BN138_227 CCO21039.1 13623 - 15042 (+) HF548280.1:32227-33646 -
- BN138_228 CCO21040.1 15046 - 16177 (+) HF548280.1:33650-34781 -
- BN138_229 CCO21041.1 16184 - 17141 (+) HF548280.1:34788-35745 -

Cluster number

1

Gene name

Gene position

Gene type

Found by CGCFinder?

- 1 - 3204 (+) TC: gnl|TC-DB|Q45780|1.B.14.6.1 Yes
- 3220 - 4896 (+) other Yes
- 4918 - 6231 (+) other Yes
- 6228 - 8558 (+) CAZyme: GH10| GH10|3.2.1.8|CBM4 Yes
- 8715 - 11087 (+) CAZyme: GH115|GH115 Yes
- 11084 - 13609 (+) CAZyme: GH11|3.2.1.8| GH11| CE20|CE20 Yes
- 13624 - 15042 (+) TC: gnl|TC-DB|P94488|2.A.2.3.2 Yes
- 15047 - 16177 (+) CAZyme: GH10| GH10|3.2.1.8 Yes
- 16185 - 17141 (+) CAZyme: GH43_1|GH43_1 Yes

PUL ID

PUL0630

PubMed

33187992, Appl Environ Microbiol. 2021 Jan 15;87(3):e01714-20. doi: 10.1128/AEM.01714-20. Print 2021 Jan 15.

Title

Multimodularity of a GH10 Xylanase Found in the Termite Gut Metagenome.

Author

Wu H, Ioannou E, Henrissat B, Montanier CY, Bozonnet S, O'Donohue MJ, Dumon C

Abstract

The functional screening of a Pseudacanthotermes militaris termite gut metagenomic library revealed an array of xylan-degrading enzymes, including P. militaris 25 (Pm25), a multimodular glycoside hydrolase family 10 (GH10). Sequence analysis showed details of the unusual domain organization of this enzyme. It consists of one catalytic domain, which is intercalated by two carbohydrate binding modules (CBMs) from family 4. The genes upstream of the genes encoding Pm25 are susC-susD-unk, suggesting Pm25 is a Xyn10C-like enzyme belonging to a polysaccharide utilization locus. The majority of Xyn10C-like enzymes shared the same interrupted domain architecture and were vastly distributed in different xylan utilization loci found in gut Bacteroidetes, indicating the importance of this enzyme in glycan acquisition for gut microbiota. To understand its unusual multimodularity and the possible role of the CBMs, a detailed characterization of the full-length Pm25 and truncated variants was performed. Results revealed that the GH10 catalytic module is specific toward the hydrolysis of xylan. Ligand binding results indicate that the GH10 module and the CBMs act independently, whereas the tandem CBM4s act synergistically with each other and improve enzymatic activity when assayed on insoluble polysaccharides. In addition, we show that the UNK protein upstream of Pm25 is able to bind arabinoxylan. Altogether, these findings contribute to a better understanding of the potential role of Xyn10C-like proteins in xylan utilization systems of gut bacteria.IMPORTANCE Xylan is the major hemicellulosic polysaccharide in cereals and contributes to the recalcitrance of the plant cell wall toward degradation. Members of the Bacteroidetes, one of the main phyla in rumen and human gut microbiota, have been shown to encode polysaccharide utilization loci dedicated to the degradation of xylan. Here, we present the biochemical characterization of a xylanase encoded by a Bacteroidetes strain isolated from the termite gut metagenome. This xylanase is a multimodular enzyme, the sequence of which is interrupted by the insertion of two CBMs from family 4. Our results show that this enzyme resembles homologues that were shown to be important for xylan degradation in rumen or human diet and show that the CBM insertion in the middle of the sequence seems to be a common feature in xylan utilization systems. This study shed light on our understanding of xylan degradation and plant cell wall deconstruction, which can be applied to several applications in food, feed, and bioeconomy.