|
|
||
|
|
|
|
|
UniProt functional annotation for Q01172 | ||
|
|
|
|
|
|
||
| UniProt code: Q01172. |
|
||
| Organism: | |
Aspergillus niger. |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Aspergillus subgen. Circumdati. |
|
||
|
||
| Function: | |
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. |
|
||
| Catalytic activity: | |
Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D- galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10; |
| Subcellular location: | |
Secreted {ECO:0000305}. |
| Ptm: | |
N-glycosylated at Asn-129 and O-glycosylated at Thr-88 when expressed in Aspergillus nidulans. The protein from strain 4M-147 is O- glycosylated at Thr-88 and Ser-368. PubMed:9195887 modeled GalNAc at the O-glycosylation site, a glycosylation not observed in fungi. The O- linked saccharide is probably mannose. |
| Similarity: | |
Belongs to the polysaccharide lyase 1 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.