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CAZyme Information: MGYG000004188_00253

You are here: Home > Sequence: MGYG000004188_00253

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;
CAZyme ID MGYG000004188_00253
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
605 MGYG000004188_1|CGC7 68815.75 5.9911
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004188 3351981 MAG United Kingdom Europe
Gene Location Start: 351181;  End: 352998  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.111 3.2.1.51

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 38 373 3.5e-83 0.9104046242774566
CBM32 487 589 1.5e-16 0.7580645161290323

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 5.82e-76 52 473 11 425
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 2.29e-40 90 371 79 327
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 1.95e-35 89 368 75 326
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.
pfam00754 F5_F8_type_C 2.51e-14 499 600 28 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd00057 FA58C 3.90e-06 494 601 30 143
Substituted updates: Jan 31, 2002

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQA10649.1 0.0 17 604 18 603
ALJ41003.1 0.0 17 604 19 604
AAO76732.1 0.0 17 604 18 603
QMW89377.1 0.0 17 604 18 603
QUT39427.1 0.0 17 604 19 604

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 0.0 19 602 1 582
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
5K9H_A 1.85e-141 51 585 38 567
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
3UES_A 3.26e-138 48 477 15 475
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UES_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3MO4_A 3.13e-136 48 477 17 477
Thecrystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3MO4_B The crystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3UET_A 4.15e-136 48 477 15 475
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UET_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GW72 5.49e-120 51 478 37 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 5.33e-117 51 473 39 471
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713 8.77e-11 90 371 92 341
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q6AYS4 2.26e-08 59 209 70 224
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
Q9VTJ4 2.42e-08 7 206 9 229
Putative alpha-L-fucosidase OS=Drosophila melanogaster OX=7227 GN=Fuca PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000001 1.000086 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004188_00253.