Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.J00367.1 |
Family | GH29 |
Protein Properties | Length: 535 Molecular Weight: 60014.8 Isoelectric Point: 6.9401 |
Chromosome | Chromosome/Scaffold: 10 Start: 3607424 End: 3610662 |
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 | 59 | 358 | 0 |
TSRQLEWQSASMALFLHFGPNTFTDSEWGSGRADPSVFHPTRLDAAQWVGVAKQAGFSRVILTAKHHDGFCLWPSEYTDYSVRSSPWRGGRGDVVAELSS AARDAGIGLGLYLSPWDRHEPSYGRTVEYNEFYVGQMTELLTRYGEIKEVWLDGAKGEGEKDMDYYFESWFSLIRQLQPRAVIFSDAGPDTRWIGDEAGV AGSTCWSAFNRSNAKIGGTDPQYSRSGDPVGQDWVPAECDVSIRPGWFWHASEVPKSARTLLDIYYKSVGRNCLLLLNVPPNSLGLISKEDVQVLQEFNE |
Full Sequence |
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Protein Sequence Length: 535 Download |
MKKKTMTSKY GKPISPNAFL SIFALSICLL SSSSVGDCLV RSADSPQKPP PLPILPIPTS 60 RQLEWQSASM ALFLHFGPNT FTDSEWGSGR ADPSVFHPTR LDAAQWVGVA KQAGFSRVIL 120 TAKHHDGFCL WPSEYTDYSV RSSPWRGGRG DVVAELSSAA RDAGIGLGLY LSPWDRHEPS 180 YGRTVEYNEF YVGQMTELLT RYGEIKEVWL DGAKGEGEKD MDYYFESWFS LIRQLQPRAV 240 IFSDAGPDTR WIGDEAGVAG STCWSAFNRS NAKIGGTDPQ YSRSGDPVGQ DWVPAECDVS 300 IRPGWFWHAS EVPKSARTLL DIYYKSVGRN CLLLLNVPPN SLGLISKEDV QVLQEFNELR 360 RSIFNENLAK SALLSASSTR GGMMNNSRFS AENVLKEGIY SYWAPEENRS DWTLYLRFQE 420 KVKFNVLQVQ EPIQLGQRVI QFHLKTLNDR GEWRQVINGT TVGYQRLLQF PMLETQELRF 480 VIDKSRADPL ISYLGLYVDT FSILTETSTN TSQTHVNGSW VIMKTARNNL SATL* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00812 | Alpha_L_fucos | 4.0e-37 | 96 | 356 | 284 | + 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 | 6.0e-38 | 64 | 356 | 329 | + Alpha-L-fucosidase. | ||
COG3669 | COG3669 | 7.0e-74 | 64 | 497 | 453 | + 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 | 48 | 514 | 28 | 494 | ATFUC1 (alpha-L-fucosidase 1); alpha-L-fucosidase [Arabidopsis thaliana] |
Swiss-Prot | Q8GW72 | 0 | 48 | 514 | 28 | 494 | 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 | 59 | 519 | 51 | 508 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002313533.1 | 0 | 59 | 502 | 15 | 457 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523703.1 | 0 | 62 | 522 | 67 | 528 | 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 | 58 | 492 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
PDB | 3ues_A | 0 | 58 | 492 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
PDB | 3mo4_B | 0 | 58 | 492 | 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 | 58 | 492 | 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 | 58 | 492 | 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 |