logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004748_01453

You are here: Home > Sequence: MGYG000004748_01453

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 MGYG000004748_01453
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
927 105104.79 7.1982
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004748 4696076 MAG China Asia
Gene Location Start: 197337;  End: 200120  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004748_01453.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 43 372 1.8e-82 0.8901734104046243
GH16 694 911 1.2e-25 0.8478260869565217

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 7.10e-69 50 476 11 430
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 1.10e-37 88 372 79 330
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 4.31e-31 88 372 76 332
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.
cd08023 GH16_laminarinase_like 8.28e-25 690 911 35 235
Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
pfam00754 F5_F8_type_C 6.21e-14 510 619 17 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QBJ17909.1 0.0 1 927 1 925
QUT89375.1 0.0 3 624 2 623
ALJ59589.1 0.0 3 624 2 623
QDO67972.1 0.0 3 624 2 623
ADV42493.1 0.0 3 625 2 624

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 2.39e-267 20 621 2 582
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 6.35e-131 49 603 38 566
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
3UES_A 1.08e-130 42 465 11 465
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]
3UET_A 1.28e-128 42 465 11 465
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 2.69e-128 42 465 13 467
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 1.52e-109 49 476 37 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.77e-106 49 476 39 476
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713 2.23e-10 75 204 82 211
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q9VTJ4 1.95e-08 87 227 111 239
Putative alpha-L-fucosidase OS=Drosophila melanogaster OX=7227 GN=Fuca PE=2 SV=2
Q6AYS4 3.15e-08 57 244 70 255
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
0.000435 0.998664 0.000218 0.000238 0.000211 0.000191

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004748_01453.