logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002171_01791

You are here: Home > Sequence: MGYG000002171_01791

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 Phocaeicola sp002493165
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp002493165
CAZyme ID MGYG000002171_01791
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
495 MGYG000002171_42|CGC1 57233.99 7.087
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002171 3793747 MAG Denmark Europe
Gene Location Start: 1117;  End: 2604  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002171_01791.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 30 339 4.7e-72 0.8583815028901735

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00812 Alpha_L_fucos 1.99e-49 43 212 29 230
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 1.56e-46 43 222 28 244
Alpha-L-fucosidase.
COG3669 AfuC 1.24e-43 30 493 11 430
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam00754 F5_F8_type_C 3.25e-08 361 487 1 121
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
QIU93293.1 1.72e-268 7 493 6 493
QEW36132.1 2.26e-261 5 495 2 491
QNA45994.1 6.96e-249 2 493 6 497
QIL40371.1 2.10e-247 10 493 16 501
ATP55793.1 3.67e-246 1 493 1 492

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 7.41e-53 30 336 32 347
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 9.74e-49 30 342 39 353
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
3UES_A 2.51e-44 30 415 19 410
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 4.63e-43 30 415 19 410
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 4.79e-43 30 415 21 412
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 1.26e-56 30 487 38 471
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.50e-45 7 492 6 475
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P10901 2.00e-16 42 199 42 239
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
C3YWU0 5.98e-15 68 326 97 330
Alpha-L-fucosidase OS=Branchiostoma floridae OX=7739 GN=BRAFLDRAFT_56888 PE=3 SV=2
P49713 3.67e-13 74 206 98 234
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 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
0.000219 0.999150 0.000177 0.000149 0.000142 0.000133

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002171_01791.