| Basic Information | |
|---|---|
| Species | Mimulus guttatus |
| Cazyme ID | mgv1a004219m |
| Family | GH29 |
| Protein Properties | Length: 540 Molecular Weight: 60641.4 Isoelectric Point: 5.3404 |
| Chromosome | Chromosome/Scaffold: 196 Start: 525444 End: 528347 |
| 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 | 60 | 368 | 0 |
| PPIPILPIPNSNQISWQLTEMAMFFHFGTNTFTDSEWGTGHADPSVFNPPSLNATQWVNAAKDSGFSRVILTVKHHDGFCLWPSEYTDYSVKSSTWRNGT GDVLRELAAAAKIAGVQLGIYLSPWDRHEPCYGKTYEYNEYYLGQMTELLTRYGEIREVFLDGAKGEGEKSMEYFFEDWFSVIHQLQPRAVIFSDAGPDT RWVGDEGGVAGITCWSLFNRSDAKIGDTDTDYSIGGDPFGHDWVPAECDVSIRPGWFWHPSESPKSALTLLDLYYKSVGRNCLLLLNVPPNSSGLISQQD IQVLKEFSD | |||
| Full Sequence |
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| Protein Sequence Length: 540 Download |
| MVKETAIDNQ QQPRRIFSTK PLKFSNPRST KHIPIILLVI ATICLKSQPS LSSSHPPPPP 60 PIPILPIPNS NQISWQLTEM AMFFHFGTNT FTDSEWGTGH ADPSVFNPPS LNATQWVNAA 120 KDSGFSRVIL TVKHHDGFCL WPSEYTDYSV KSSTWRNGTG DVLRELAAAA KIAGVQLGIY 180 LSPWDRHEPC YGKTYEYNEY YLGQMTELLT RYGEIREVFL DGAKGEGEKS MEYFFEDWFS 240 VIHQLQPRAV IFSDAGPDTR WVGDEGGVAG ITCWSLFNRS DAKIGDTDTD YSIGGDPFGH 300 DWVPAECDVS IRPGWFWHPS ESPKSALTLL DLYYKSVGRN CLLLLNVPPN SSGLISQQDI 360 QVLKEFSDLR NSIFTLNLAK NATISANSTR GKTGDSRYGP RNVLEEGIYS YWAPNRSISE 420 WILYLDFEEA VTFNVLLLQE PIQMGQRIIE FHLDFLNEGG EWEVVTGGTT VGYKRLLLFP 480 SVKASRLRVV IDESRADPLV SYLGIYFDPF SISGQVSKIF NGSEVLQQTT RRNSSTYYV* 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 | 2.0e-31 | 106 | 366 | 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 | 2.0e-31 | 82 | 366 | 321 | + Alpha-L-fucosidase. | ||
| COG3669 | COG3669 | 5.0e-62 | 75 | 506 | 443 | + Alpha-L-fucosidase [Carbohydrate transport and metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004560 | alpha-L-fucosidase activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0007155 | cell adhesion |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | NP_180377.2 | 0 | 59 | 515 | 29 | 486 | ATFUC1 (alpha-L-fucosidase 1); alpha-L-fucosidase [Arabidopsis thaliana] |
| Swiss-Prot | Q8GW72 | 0 | 59 | 515 | 29 | 486 | 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 | 70 | 517 | 52 | 495 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002313533.1 | 0 | 70 | 511 | 16 | 457 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523703.1 | 0 | 72 | 512 | 67 | 508 | 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 | 68 | 501 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
| PDB | 3ues_A | 0 | 68 | 501 | 19 | 471 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
| PDB | 3mo4_B | 0 | 68 | 501 | 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 | 68 | 501 | 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 | 68 | 501 | 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| DY270181 | 284 | 75 | 358 | 0 |
| DY300194 | 288 | 97 | 384 | 0 |
| DY291901 | 279 | 75 | 353 | 0 |
| DY272403 | 294 | 75 | 367 | 0 |
| DY300194 | 29 | 75 | 103 | 0.000005 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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