The domain within your query sequence starts at position 41 and ends at position 413; the E-value for the Melibiase_2 domain shown below is 3.5e-190.
TPTMGWLHWERFMCNLDCQEEPDACISEQLFMQMAELMVSDGWRDAGYDYLCIDDCWMAP ERDSKGRLQADPQRFPSGIKHLANYVHSKGLKLGIYADVGNKTCAGFPGSFGSYDIDAQT FADWGVDLLKFDGCHCDSVVSLENGYKYMALALNRTGRSIVYSCEWPLYLRPFHKPNYTD IQYYCNHWRNFDDVYDSWESIKNILSWTVVYQKEIVEVAGPGSWNDPDMLVIGNFGLSWD QQVTQMALWAIMAAPLLMSNDLRQISSQAKALLQNKDVIAINQDPLGKQGYCFRKENHIE VWERPLSNLAWAVAVRNLQEIGGPCPYTIQISSLGRGLACNPGCIITQLLPEKVHLGFYE WTLTLKTRVNPSG
Melibiase_2 |
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PFAM accession number: | PF16499 |
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Interpro abstract (IPR002241): | O-Glycosyl hydrolases ( EC 3.2.1. ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ (PUBMED:7624375) (PUBMED:8535779) ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website. Glycoside hydrolase family 27 comprises enzymes with several known activities; alpha-galactosidase ( EC 3.2.1.22 ); alpha-N-acetylgalactosaminidase ( EC 3.2.1.49 ); isomalto-dextranase ( EC 3.2.1.94 ). Alpha-galactosidase (melibiase) catalyses the hydrolysis of melibiose into galactose and glucose [ (PUBMED:7725791) ]. In man, deficiency in the enzyme results in Fabry's disease (X-linked sphingolipidosis). Alpha-N-acetylgalactosaminidase catalyses the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D-galactosaminides [ (PUBMED:2174888) ]. Two conserved Asp residues may be involved in the catalytic mechanism in these enzymes. Deficiency in this enzyme results in Schindler and Kanzaki diseases. |
GO process: | carbohydrate metabolic process (GO:0005975) |
GO function: | hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Melibiase_2