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UniProt functional annotation for Q0TR53 | ||
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| UniProt code: Q0TR53. |
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| Organism: | |
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A). |
| Taxonomy: | |
Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; Clostridium. |
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| Function: | |
Binds carbohydrates (PubMed:16990278). Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals. {ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:16990278, ECO:0000269|PubMed:18721751}. |
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| Catalytic activity: | |
Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = L-seryl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48876, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:90838, ChEBI:CHEBI:506227; EC=3.2.1.169; Evidence={ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:18721751, ECO:0000269|PubMed:22365600}; |
| Catalytic activity: | |
Reaction=3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O = L-threonyl-[protein] + N-acetyl-D-glucosamine; Xref=Rhea:RHEA:48892, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:90840, ChEBI:CHEBI:506227; EC=3.2.1.169; Evidence={ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:18721751, ECO:0000269|PubMed:22365600}; |
| Activity regulation: | |
Inhibited by O-(2-acetamido-2-deoxy-D- glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc) and streptozotocin. {ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:18721751}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=2.9 uM for 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide (4MU-NAG) {ECO:0000269|PubMed:16541109}; |
| Miscellaneous: | |
Metal-binding observed in X-ray crystal structures is artifactual. {ECO:0000305}. |
| Similarity: | |
Belongs to the glycosyl hydrolase 84 family. {ECO:0000255}. |
Annotations taken from UniProtKB at the EBI.