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CAZyme Information: MGYG000001503_00309

You are here: Home > Sequence: MGYG000001503_00309

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 Fermentimonas caenicola
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Fermentimonas; Fermentimonas caenicola
CAZyme ID MGYG000001503_00309
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
741 MGYG000001503_1|CGC3 84696.38 5.3952
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001503 2824716 Isolate not provided not provided
Gene Location Start: 375321;  End: 377546  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001503_00309.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 60 391 7.3e-73 0.8294797687861272
CBM32 619 738 1.4e-18 0.8790322580645161

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 1.98e-56 50 510 11 428
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 7.88e-32 94 391 85 326
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 7.56e-29 94 391 82 328
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.
pfam00754 F5_F8_type_C 4.19e-22 614 738 2 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd00057 FA58C 3.82e-12 617 725 18 130
Substituted updates: Jan 31, 2002

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CEA16338.1 0.0 1 741 1 741
SCD22150.1 0.0 1 741 1 742
QRX62814.1 0.0 1 741 1 741
ATA92697.1 0.0 28 741 20 733
AEK23001.1 0.0 2 741 7 745

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 5.09e-106 30 724 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 1.35e-90 46 511 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 1.08e-89 46 511 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 1.51e-88 46 511 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 5.57e-71 39 512 23 463
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 1.57e-68 49 515 37 480
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 5.25e-64 49 507 39 471
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P10901 3.52e-10 88 391 100 351
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
P49713 1.57e-06 88 396 92 345
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q9VTJ4 2.11e-06 58 174 81 189
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000307 0.999052 0.000169 0.000159 0.000145 0.000143

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001503_00309.