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CAZyme Information: MGYG000001975_02020

You are here: Home > Sequence: MGYG000001975_02020

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 Prevotella sp900552515
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900552515
CAZyme ID MGYG000001975_02020
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
449 51542.67 7.0071
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001975 2921145 MAG Denmark Europe
Gene Location Start: 4924;  End: 6273  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001975_02020.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 24 339 1.3e-99 0.9190751445086706

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00812 Alpha_L_fucos 2.73e-132 27 378 8 383
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 3.02e-121 29 335 9 333
Alpha-L-fucosidase.
COG3669 AfuC 3.58e-43 50 342 1 324
Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCQ40555.1 1.00e-268 18 449 19 449
AKA50907.1 1.42e-268 18 449 19 449
ANQ59545.1 1.42e-268 18 449 19 449
CAH06554.1 1.42e-268 18 449 19 449
CBW21439.1 1.42e-268 18 449 19 449

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GN6_A 8.46e-80 33 433 27 444
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]
2WVS_A 1.26e-51 27 414 11 434
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]
6HZY_A 2.46e-51 19 414 21 455
Crystalstructure of a bacterial fucosidase with inhibitor FucPUG [Bacteroides thetaiotaomicron VPI-5482],6HZY_B Crystal structure of a bacterial fucosidase with inhibitor FucPUG [Bacteroides thetaiotaomicron VPI-5482]
4WSK_A 3.04e-51 18 414 20 453
Crystalstructure of a bacterial fucosidase with phenyl((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)methanone [Bacteroides thetaiotaomicron VPI-5482],4WSK_B Crystal structure of a bacterial fucosidase with phenyl((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)methanone [Bacteroides thetaiotaomicron VPI-5482],4WSK_C Crystal structure of a bacterial fucosidase with phenyl((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)methanone [Bacteroides thetaiotaomicron VPI-5482],4WSK_D Crystal structure of a bacterial fucosidase with phenyl((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)methanone [Bacteroides thetaiotaomicron VPI-5482]
4PCS_A 3.15e-51 27 414 7 430
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q99KR8 5.56e-47 29 340 31 364
Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
P48300 6.01e-47 38 421 51 448
Tissue alpha-L-fucosidase OS=Canis lupus familiaris OX=9615 GN=FUCA1 PE=2 SV=1
Q2KIM0 6.37e-47 39 341 55 376
Tissue alpha-L-fucosidase OS=Bos taurus OX=9913 GN=FUCA1 PE=2 SV=1
Q60HF8 8.85e-47 39 418 54 448
Tissue alpha-L-fucosidase OS=Macaca fascicularis OX=9541 GN=FUCA1 PE=2 SV=1
Q99LJ1 9.01e-47 39 377 38 397
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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.076055 0.909593 0.007917 0.002474 0.001547 0.002378

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001975_02020.