| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G019783_T01 |
| Family | GH29 |
| Protein Properties | Length: 514 Molecular Weight: 56648.1 Isoelectric Point: 4.6703 |
| Chromosome | Chromosome/Scaffold: 2 Start: 17986668 End: 17998162 |
| Description | alpha-L-fucosidase 1 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH29 | 40 | 335 | 0 |
| QLRWQLSEMALFLHFGPNTFTDSEWGTGHADPSVFAPSALDAGQWARIAAQGGFGRVVLTAKHHDGFCLWPSALTEYSVAASPWQGGAGDVVAELAAAAR AEGLGLGLYLSPWDRHEPVYGDTIAYNEHYLGQMTELLTRYGDVEEVWLDGAKGDAKKMDYMFDAWFSLIHQLQERVVIFSDAGPDTRWVGDEAGVAGYT CWSPFNKSSVTIGHTTAEYSSSGDPFGQDWVPAECDVSIRPGWFWHASEKPKNVTTLLDIYYKSVGRNCLLILNVPPNSSGLIADEDIQVLQEFTE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 514 Download |
| MAALVPLLLA HLLLCVHGAT VTSVATPPPL PVLPVPSYAQ LRWQLSEMAL FLHFGPNTFT 60 DSEWGTGHAD PSVFAPSALD AGQWARIAAQ GGFGRVVLTA KHHDGFCLWP SALTEYSVAA 120 SPWQGGAGDV VAELAAAARA EGLGLGLYLS PWDRHEPVYG DTIAYNEHYL GQMTELLTRY 180 GDVEEVWLDG AKGDAKKMDY MFDAWFSLIH QLQERVVIFS DAGPDTRWVG DEAGVAGYTC 240 WSPFNKSSVT IGHTTAEYSS SGDPFGQDWV PAECDVSIRP GWFWHASEKP KNVTTLLDIY 300 YKSVGRNCLL ILNVPPNSSG LIADEDIQVL QEFTEIRRAI FSQNFAANAT VTANSVRGEQ 360 DNLQFAPSKV LEDGIYSYWA PQEGQTCWEM LFDLGQSTSF NLLQLQEPIQ LGQRVIEFHV 420 AILVDELWQT IVEGTTIGYK RLLLFPVTES RYLKLTIDSA RADPLISFFG VFMDPFSSIH 480 SLQNHVKPPR TNSNEVTMLR MAHASVNKSI DAM* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00812 | Alpha_L_fucos | 7.0e-22 | 74 | 335 | 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-22 | 74 | 335 | 276 | + Alpha-L-fucosidase. | ||
| COG3669 | COG3669 | 2.0e-55 | 40 | 472 | 444 | + Alpha-L-fucosidase [Carbohydrate transport and metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004560 | alpha-L-fucosidase activity |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACG47369.1 | 0 | 1 | 513 | 1 | 513 | alpha-L-fucosidase 1 precursor [Zea mays] |
| EMBL | CAH68057.1 | 0 | 17 | 513 | 21 | 517 | B0103C08-B0602B01.14 [Oryza sativa (indica cultivar-group)] |
| RefSeq | NP_001053546.1 | 0 | 17 | 513 | 21 | 517 | Os04g0560400 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001131532.1 | 0 | 1 | 513 | 1 | 513 | hypothetical protein LOC100192871 [Zea mays] |
| RefSeq | XP_002448322.1 | 0 | 17 | 513 | 17 | 513 | hypothetical protein SORBIDRAFT_06g025200 [Sorghum bicolor] |
| 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 | 467 | 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 | 467 | 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 | 467 | 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 | 467 | 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 | 467 | 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 |
