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CAZyme Information: MGYG000001489_01170

You are here: Home > Sequence: MGYG000001489_01170

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 Parabacteroides goldsteinii
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii
CAZyme ID MGYG000001489_01170
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
715 MGYG000001489_1|CGC28 80910.88 6.5619
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001489 6453137 Isolate not provided not provided
Gene Location Start: 1500744;  End: 1502891  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001489_01170.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 60 393 1.8e-73 0.8352601156069365

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 1.24e-55 51 506 11 425
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 5.41e-32 66 392 30 326
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 1.58e-29 66 392 31 328
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.
pfam13287 Fn3_assoc 1.85e-09 550 590 4 45
Fn3 associated.
pfam13290 CHB_HEX_C_1 2.52e-09 553 600 18 67
Chitobiase/beta-hexosaminidase C-terminal domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT50205.1 0.0 1 714 1 712
SCD22150.1 0.0 1 715 1 742
QTO26413.1 0.0 1 714 1 736
QCQ30568.1 0.0 1 714 1 736
QRO25056.1 0.0 9 714 18 749

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 1.26e-115 31 699 12 566
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
3UES_A 7.75e-100 47 510 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 6.32e-99 47 510 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 9.01e-98 47 510 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]
5K9H_A 3.13e-79 50 714 38 583
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GW72 1.76e-73 50 511 37 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.28e-68 49 506 36 471
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713 1.08e-09 87 397 90 345
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q99LJ1 3.05e-09 89 430 96 381
Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca1 PE=1 SV=1
P17164 5.48e-09 89 430 106 391
Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1

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 0.000000 1.000082 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001489_01170.