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CAZyme Information: MGYG000003252_05754

You are here: Home > Sequence: MGYG000003252_05754

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 Bacteroides sp900761785
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900761785
CAZyme ID MGYG000003252_05754
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
469 MGYG000003252_569|CGC1 54458.15 7.7041
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003252 8296673 MAG United States North America
Gene Location Start: 5779;  End: 7188  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003252_05754.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 35 380 1.4e-102 0.9277456647398844

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01120 Alpha_L_fucos 4.88e-114 37 376 3 333
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 8.17e-102 34 407 1 370
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.
COG3669 AfuC 7.03e-42 65 387 1 328
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam16757 Fucosidase_C 1.83e-04 389 460 6 79
Alpha-L-fucosidase C-terminal domain. The C-terminal domain of Structure 1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRQ59033.1 0.0 1 469 1 469
SCV10806.1 0.0 1 469 4 472
ALJ46449.1 0.0 1 469 4 472
QNL41433.1 0.0 1 468 1 468
QRO24330.1 3.08e-216 1 465 1 459

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GN6_A 5.17e-68 50 405 29 376
Alpha-L-fucosidaseisoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_B Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_C Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_D Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_E Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_F Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus]
4JL2_A 3.39e-47 45 466 16 434
Crystalstructure of a bacterial fucosidase with a monovalent iminocyclitol inhibitor [Bacteroides thetaiotaomicron VPI-5482],4JL2_B Crystal structure of a bacterial fucosidase with a monovalent iminocyclitol inhibitor [Bacteroides thetaiotaomicron VPI-5482]
4PCS_A 5.26e-47 45 466 16 434
Crystalstructure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_B Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_C Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_D Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_A Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_B Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_C Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_D Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482]
2WVT_A 5.70e-47 45 466 20 438
Crystalstructure of an alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron in complex with a novel iminosugar fucosidase inhibitor [Bacteroides thetaiotaomicron VPI-5482],2WVT_B Crystal structure of an alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron in complex with a novel iminosugar fucosidase inhibitor [Bacteroides thetaiotaomicron VPI-5482],2WVU_A Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_B Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_C Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_D Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482]
2WVS_A 5.70e-47 45 466 20 438
Crystalstructure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_B Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_C Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_D Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5RFI5 2.80e-38 37 407 29 397
Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1
Q9BTY2 3.99e-38 37 407 31 399
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q6AYS4 4.58e-37 39 454 25 439
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
Q99KR8 4.73e-37 39 407 27 393
Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q9VTJ4 2.52e-35 36 453 30 473
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
0.001011 0.997782 0.000365 0.000303 0.000270 0.000257

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003252_05754.