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CAZyme Information: MGYG000002637_00199

You are here: Home > Sequence: MGYG000002637_00199

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 Prevotella jejuni
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella jejuni
CAZyme ID MGYG000002637_00199
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
509 MGYG000002637_2|CGC3 57299.85 6.8252
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002637 2560086 MAG China Asia
Gene Location Start: 69080;  End: 70609  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 34 362 7.2e-58 0.9132947976878613
CBM32 376 495 2.9e-17 0.8467741935483871

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 3.31e-35 43 509 4 430
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 1.03e-25 61 362 44 329
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 4.29e-21 46 362 36 331
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 1.27e-13 374 496 1 114
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd00057 FA58C 0.002 375 493 14 127
Substituted updates: Jan 31, 2002

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB79996.1 0.0 1 509 1 509
QUB82373.1 0.0 1 509 1 509
AUI56213.1 0.0 1 509 1 509
QUB69927.1 0.0 1 509 1 508
QUB66849.1 0.0 1 509 1 508

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5K9H_A 2.40e-92 45 509 34 463
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
3UES_A 2.05e-74 50 507 19 474
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]
4ZRX_A 2.72e-73 49 509 31 458
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
3UET_A 2.34e-72 50 507 19 474
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]
3MO4_A 7.25e-71 50 507 21 476
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GW72 3.01e-83 43 509 31 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 4.19e-78 43 509 33 476
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
Q6AYS4 6.48e-07 46 362 55 353
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.001532 0.997064 0.000307 0.000412 0.000334 0.000297

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002637_00199.