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CAZyme Information: MGYG000000201_03819

You are here: Home > Sequence: MGYG000000201_03819

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 Blautia_A sp900066145
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900066145
CAZyme ID MGYG000000201_03819
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
436 MGYG000000201_20|CGC2 50447.1 5.0676
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000201 4593677 Isolate China Asia
Gene Location Start: 38092;  End: 39402  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.51

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 6 337 1.7e-116 0.8872832369942196

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00812 Alpha_L_fucos 1.23e-120 6 366 17 374
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 1.25e-118 3 333 11 333
Alpha-L-fucosidase.
COG3669 AfuC 3.68e-49 22 337 1 321
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam14871 GHL6 5.19e-09 59 144 1 80
Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases.
PRK02227 PRK02227 0.006 59 123 132 185
(5-formylfuran-3-yl)methyl phosphate synthase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASU31305.1 1.80e-306 1 435 1 435
QQQ91849.1 1.80e-306 1 435 1 435
ANU74314.1 1.80e-306 1 435 1 435
QJU15640.1 1.48e-305 1 435 1 435
QRT29182.1 1.78e-262 1 435 1 435

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GN6_A 1.80e-203 7 436 29 446
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 1.91e-78 12 366 22 379
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]
2WVS_A 2.22e-78 12 366 26 383
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]
4PCS_A 5.57e-78 12 366 22 379
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 6.21e-78 12 366 26 383
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10901 1.12e-45 11 366 36 394
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
Q5RFI5 4.35e-41 4 336 40 366
Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1
Q9BTY2 4.50e-41 4 336 42 368
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q6AYS4 1.04e-40 6 336 36 360
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
Q99KR8 5.50e-40 6 336 38 362
Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.965984 0.031375 0.002437 0.000060 0.000050 0.000098

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000201_03819.