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CAZyme Information: MGYG000001878_00825

You are here: Home > Sequence: MGYG000001878_00825

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 sp900548175
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900548175
CAZyme ID MGYG000001878_00825
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
683 77139.6 5.6666
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001878 3414068 MAG Denmark Europe
Gene Location Start: 22861;  End: 24912  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001878_00825.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 36 336 2.2e-76 0.8323699421965318

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 3.90e-56 39 463 15 413
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 2.85e-36 62 333 69 315
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 2.17e-35 70 333 73 317
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 1.23e-17 499 558 1 59
Fn3 associated.
pfam13290 CHB_HEX_C_1 4.93e-13 489 545 2 58
Chitobiase/beta-hexosaminidase C-terminal domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT97698.1 0.0 21 683 19 685
AST55451.1 0.0 21 683 19 685
QJE29484.1 0.0 21 683 19 685
QIX64728.1 0.0 21 683 19 685
QCY57860.1 0.0 21 683 19 685

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5K9H_A 8.74e-158 30 665 34 569
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
4ZRX_A 4.74e-117 34 680 31 582
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
3EYP_A 4.48e-113 29 480 4 454
Crystalstructure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],3EYP_B Crystal structure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],4OUE_A Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OUE_B Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_A Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_B Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482]
3UES_A 9.56e-100 35 461 19 457
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 6.03e-98 35 461 21 459
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 7.24e-105 26 498 29 500
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.18e-102 4 524 3 515
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
Q9BTY2 4.18e-10 73 191 107 232
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q5RFI5 9.63e-10 73 191 105 230
Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1
Q99LJ1 2.85e-09 81 333 104 335
Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 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 0.000001 1.000032 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001878_00825.