Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10016468m |
Family | GH29 |
Protein Properties | Length: 553 Molecular Weight: 62257.3 Isoelectric Point: 5.9682 |
Chromosome | Chromosome/Scaffold: 10 Start: 3357963 End: 3360443 |
Description | alpha-L-fucosidase 1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH29 | 83 | 380 | 0 |
SQQLQWQLGSMAMFLHFGPNTFTDSEWGSGKADPSVFNPTHLNATQWVQIAKDSGFSRVILTAKHHDGFCLWPSEYTDYSVKSSPWRAGTGDVVAELASA AAAAGIGLGLYLSPWDRHEGSYGETLGYNEYYLSQMTELLTKYGEIKEVWLDGAKGKGEKYMEYFFDTWFSLIHQLQPGAVIFSDAGPDVRYIGNENGVA GSTCWSLFNRTNAKIGGTDPLYSLEGDGFGQDWVPAECDISIRPGWFWHALESPKPAVQLLDIYYNTVGRNCLFLLNVPPNSSGLISEQDIKVLEEFR |
Full Sequence |
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Protein Sequence Length: 553 Download |
MNVTSKHQLE IFSTKDTTRL HSRTEEDEEI VEEKNPLQSS RPMSLITHFF FFFFVFSIVS 60 LFKISNSTPL KPHPLPILPL PSSQQLQWQL GSMAMFLHFG PNTFTDSEWG SGKADPSVFN 120 PTHLNATQWV QIAKDSGFSR VILTAKHHDG FCLWPSEYTD YSVKSSPWRA GTGDVVAELA 180 SAAAAAGIGL GLYLSPWDRH EGSYGETLGY NEYYLSQMTE LLTKYGEIKE VWLDGAKGKG 240 EKYMEYFFDT WFSLIHQLQP GAVIFSDAGP DVRYIGNENG VAGSTCWSLF NRTNAKIGGT 300 DPLYSLEGDG FGQDWVPAEC DISIRPGWFW HALESPKPAV QLLDIYYNTV GRNCLFLLNV 360 PPNSSGLISE QDIKVLEEFR EIKTSVFSNN LARKAAVNSS SVRGGQSSKF GPKNVLEEGL 420 DKYWAPEEKQ KEWELYFEFQ DSVSFNVLEV QEPIQMGQRV ASFHLETRNI GSGKWTRVVN 480 GTTVGLKRLL RFPRVESRSL KLVVDKARTD PLISYVGIYM DKFSVSSRNS SKITITRTLQ 540 EEQQLISERL TT* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00812 | Alpha_L_fucos | 2.0e-24 | 119 | 379 | 282 | + 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 | 9.0e-30 | 95 | 379 | 320 | + Alpha-L-fucosidase. | ||
COG3669 | COG3669 | 1.0e-58 | 96 | 519 | 438 | + Alpha-L-fucosidase [Carbohydrate transport and metabolism] |
Gene Ontology | |
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GO Term | Description |
GO:0004560 | alpha-L-fucosidase activity |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_180377.2 | 0 | 71 | 545 | 28 | 503 | ATFUC1 (alpha-L-fucosidase 1); alpha-L-fucosidase [Arabidopsis thaliana] |
Swiss-Prot | Q8GW72 | 0 | 71 | 545 | 28 | 503 | FUCO1_ARATH RecName: Full=Alpha-L-fucosidase 1; AltName: Full=Alpha-L-fucoside fucohydrolase; AltName: Full=Alpha-1,3/4-fucosidase; Short=AtFUC1; Flags: Precursor |
RefSeq | XP_002276131.1 | 0 | 82 | 527 | 51 | 492 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002313533.1 | 0 | 82 | 524 | 15 | 457 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523703.1 | 0 | 82 | 527 | 64 | 510 | alpha-l-fucosidase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ues_B | 0 | 81 | 514 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
PDB | 3ues_A | 0 | 81 | 514 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
PDB | 3mo4_B | 0 | 81 | 514 | 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 | 81 | 514 | 21 | 473 | A Chain A, The Crystal Structure Of An Alpha-(1-3,4)-Fucosidase From Bifidobacterium Longum Subsp. Infantis Atcc 15697 |
PDB | 3uet_B | 0 | 81 | 514 | 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 |