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CAZyme Information: MGYG000003856_00227

You are here: Home > Sequence: MGYG000003856_00227

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 Paramuribaculum sp900551515
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900551515
CAZyme ID MGYG000003856_00227
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
589 MGYG000003856_5|CGC1 65973.6 5.6907
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003856 2220083 MAG United States North America
Gene Location Start: 35849;  End: 37618  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003856_00227.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 49 370 2.3e-79 0.8728323699421965

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 2.52e-68 49 455 11 430
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
smart00812 Alpha_L_fucos 1.86e-33 86 370 75 333
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 1.90e-32 85 370 77 331
Alpha-L-fucosidase.
pfam00754 F5_F8_type_C 6.66e-12 484 581 30 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd00057 FA58C 0.007 485 565 42 127
Substituted updates: Jan 31, 2002

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANU62713.1 1.12e-229 25 584 27 597
ASB36791.1 1.12e-229 25 584 27 597
QQR09949.1 1.34e-229 25 584 32 602
QDH57006.1 5.83e-216 25 584 27 602
QUT30237.1 1.17e-215 25 584 27 602

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 1.92e-208 25 561 8 560
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 2.30e-125 35 454 5 475
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 1.09e-123 35 454 7 477
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 2.89e-123 35 454 5 475
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 2.68e-110 48 583 38 585
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 1.01e-112 52 455 41 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 3.55e-99 53 484 44 505
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713 2.57e-10 72 363 74 341
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
P10901 5.35e-09 85 370 98 356
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
C3YWU0 9.10e-09 86 203 91 214
Alpha-L-fucosidase OS=Branchiostoma floridae OX=7739 GN=BRAFLDRAFT_56888 PE=3 SV=2

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
0.073141 0.919252 0.003209 0.002971 0.000795 0.000598

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003856_00227.