| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 481700 |
| Family | GH29 |
| Protein Properties | Length: 504 Molecular Weight: 56824.3 Isoelectric Point: 5.9914 |
| Chromosome | Chromosome/Scaffold: 4 Start: 12052272 End: 12054018 |
| Description | alpha-L-fucosidase 1 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH29 | 37 | 336 | 0 |
| SSQQLQWQLGSIAMFLHFGPNTFTNSEWGTGKANPSVFNPTHLNASQWVQIAKDSGFSRVILTAKHHDGFCLWPSEYTDYSVKSSSWRNGTGDVVAELAA AAAEAGIGLGLYLSPWDRHDQSYGKTLEYNEFYLSQMTELLTKYGEIKEVWLDGAKGEGEKDMEYFFDTWFSLIHQLQPKAVIFSDAGPDVRWIGDEAGL AGSTCWSLFNRTNAKIGDTDPLYSQEGDKFGQDWVPAECDVSIRPGWFWHALESPKPAVKLLDIYYYSVGRNCLFLLNVPPNSSGLISEQDIKVLEEFRE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 504 Download |
| MNSQITLLFF FSILCLSQIS NSSPLKPHPL PILPLPSSQQ LQWQLGSIAM FLHFGPNTFT 60 NSEWGTGKAN PSVFNPTHLN ASQWVQIAKD SGFSRVILTA KHHDGFCLWP SEYTDYSVKS 120 SSWRNGTGDV VAELAAAAAE AGIGLGLYLS PWDRHDQSYG KTLEYNEFYL SQMTELLTKY 180 GEIKEVWLDG AKGEGEKDME YFFDTWFSLI HQLQPKAVIF SDAGPDVRWI GDEAGLAGST 240 CWSLFNRTNA KIGDTDPLYS QEGDKFGQDW VPAECDVSIR PGWFWHALES PKPAVKLLDI 300 YYYSVGRNCL FLLNVPPNSS GLISEQDIKV LEEFREMTHT IFSNNLARKA LVNSSSIRGG 360 QSSQFGPKNV LEEGLDKYWA PEESQKEWVL YFEFKDSVSF NVLEIREPIQ MGQRIASFHL 420 ETRKTGSGKW ERVVSGTTVG NKRLLRFLKV ESRSLKLVVD KARTDPLISY LGIYMDKFSV 480 SSQNTSKITI TRTLKEEQQL HDL* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00812 | Alpha_L_fucos | 3.0e-24 | 50 | 334 | 328 | + Alpha-L-fucosidase. 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. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis. | ||
| pfam01120 | Alpha_L_fucos | 1.0e-26 | 50 | 334 | 319 | + Alpha-L-fucosidase. | ||
| COG3669 | COG3669 | 3.0e-57 | 51 | 474 | 434 | + Alpha-L-fucosidase [Carbohydrate transport and metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004560 | alpha-L-fucosidase activity |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3mo4_B | 0 | 36 | 469 | 21 | 473 | A Chain A, The Crystal Structure Of An Alpha-(1-3,4)-Fucosidase From Bifidobacterium Longum Subsp. Infantis Atcc 15697 |
| PDB | 3mo4_A | 0 | 36 | 469 | 21 | 473 | A Chain A, The Crystal Structure Of An Alpha-(1-3,4)-Fucosidase From Bifidobacterium Longum Subsp. Infantis Atcc 15697 |
| PDB | 3ues_B | 0 | 36 | 469 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
| PDB | 3ues_A | 0 | 36 | 469 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
| PDB | 3uet_B | 0 | 36 | 469 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
