Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Methods
Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum.
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Cloning and sequencing of xynZ gene encoding 837 amino acid polypeptide
"The putative xynZ gene was 2,511 base pairs long and encoded a polypeptide of 837 amino acids"
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Identification of duplicated 24 amino acid segment (residues 429-488) similar to C. thermocellum endoglucanases - this is the dockerin domain
"A region of 60 amino acids containing a duplicated segment of 24 amino acids was found between residues 429 and 488 of xylanase Z. This region was strongly similar to the conserved domain found at the carboxy-terminal ends of C. thermocellum endoglucanases A, B, and D"
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Deletion analysis showing active site in C-terminal half of protein (GH10 domain)
"Deletions removing up to 508 codons from the 5' end of the gene did not affect the activity of the encoded polypeptide, showing that the active site was located in the C-terminal half of the protein"
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Expression of xylanase activity in E. coli
"Expression of xylanase activity in Escherichia coli was increased up to 220-fold by fusing fragments containing the 3' end of the gene with the start of lacZ present in pUC19"
A common protein fold and similar active site in two distinct families of beta-glycanases.
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X-ray crystal structure of GH10 domain (residues 515-837) at 1.4 angstrom resolution
"The structure of the catalytic core of xylanase XynZ, which belongs to xylanase family F, has been determined at 1.4 A resolution"
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Structural characterization of the catalytic domain
"In spite of significant differences in substrate specificity and structure (including the absence of the helical subdomain), the general polypeptide folding pattern, architecture of the active site and catalytic mechanism of XynZ and CelC are similar, suggesting a common evolutionary origin"
Deep research synthesis on XynZ function and domain architecture
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XynZ is a multi-domain cellulosomal enzyme with CE1-CBM6-Dockerin I-GH10 architecture
"Domain architecture: XynZ is reported as CE1 (feruloyl esterase) - CBM6 - Dockerin type I - GH10 endo-beta-1,4-xylanase"
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The GH10 domain catalyzes endo-1,4-beta-xylanase activity (EC 3.2.1.8)
"The GH10 domain is the catalytic xylanase module (EC 3.2.1.8)"
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The CE1 domain provides feruloyl esterase activity for removing decorations from xylan
"The N-terminal CE1 in XynZ confers feruloyl esterase-type activity consistent with removal of ferulate/acetyl decorations that hinder backbone hydrolysis in plant xylans"
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The protein is localized to the cellulosome via its dockerin domain
"XynZ is exported and assembled into the cellulosome (extracellular) through its dockerin I"