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CAZyme Information: MGYG000003695_03054

You are here: Home > Sequence: MGYG000003695_03054

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 Ruminococcus_A sp003011855
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Ruminococcus_A; Ruminococcus_A sp003011855
CAZyme ID MGYG000003695_03054
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
460 53228.12 4.7001
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003695 3472119 Isolate China Asia
Gene Location Start: 2782;  End: 4164  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003695_03054.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 13 370 2e-96 0.9479768786127167

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01120 Alpha_L_fucos 1.18e-94 21 366 2 333
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 6.94e-87 38 405 21 380
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 2.76e-34 97 372 49 323
Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUH29765.1 6.04e-210 6 458 8 459
QOV20717.1 1.04e-206 8 459 3 452
BCJ95052.1 1.62e-206 9 459 46 495
ANS76896.1 1.13e-205 7 458 19 470
BCJ97219.1 1.56e-205 8 459 30 479

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GN6_A 4.98e-65 34 392 27 375
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]
1HL8_A 1.03e-46 38 460 22 449
CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL8_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL9_A Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8],1HL9_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8]
1ODU_A 1.98e-46 38 460 22 449
CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8],1ODU_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8]
2ZWY_A 2.23e-46 38 460 22 449
alpha-L-fucosidase[Thermotoga maritima],2ZWY_B alpha-L-fucosidase [Thermotoga maritima],2ZWZ_A alpha-L-fucosidase complexed with inhibitor, Core1 [Thermotoga maritima],2ZWZ_B alpha-L-fucosidase complexed with inhibitor, Core1 [Thermotoga maritima],2ZX5_A alpha-L-fucosidase complexed with inhibitor, F10 [Thermotoga maritima],2ZX5_B alpha-L-fucosidase complexed with inhibitor, F10 [Thermotoga maritima],2ZX6_A alpha-L-fucosidase complexed with inhibitor, F10-1C [Thermotoga maritima],2ZX6_B alpha-L-fucosidase complexed with inhibitor, F10-1C [Thermotoga maritima],2ZX7_A alpha-L-fucosidase complexed with inhibitor, F10-2C [Thermotoga maritima],2ZX7_B alpha-L-fucosidase complexed with inhibitor, F10-2C [Thermotoga maritima],2ZX8_A alpha-L-fucosidase complexed with inhibitor, F10-2C-O [Thermotoga maritima],2ZX8_B alpha-L-fucosidase complexed with inhibitor, F10-2C-O [Thermotoga maritima],2ZX9_A alpha-L-fucosidase complexed with inhibitor, B4 [Thermotoga maritima],2ZX9_B alpha-L-fucosidase complexed with inhibitor, B4 [Thermotoga maritima],2ZXA_A alpha-L-fucosidase complexed with inhibitor, FNJ-acetyl [Thermotoga maritima],2ZXA_B alpha-L-fucosidase complexed with inhibitor, FNJ-acetyl [Thermotoga maritima],2ZXB_A alpha-L-fucosidase complexed with inhibitor, ph-6FNJ [Thermotoga maritima],2ZXB_B alpha-L-fucosidase complexed with inhibitor, ph-6FNJ [Thermotoga maritima],2ZXD_A alpha-L-fucosidase complexed with inhibitor, iso-6FNJ [Thermotoga maritima],2ZXD_B alpha-L-fucosidase complexed with inhibitor, iso-6FNJ [Thermotoga maritima]
4PCS_A 6.06e-46 40 394 22 374
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
Q6AYS4 1.97e-32 39 416 41 400
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
Q99KR8 7.15e-32 39 416 43 402
Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q60HF8 1.79e-30 39 459 54 463
Tissue alpha-L-fucosidase OS=Macaca fascicularis OX=9541 GN=FUCA1 PE=2 SV=1
P17164 3.12e-30 39 459 48 457
Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1
Q9BTY2 3.31e-30 39 371 49 370
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2

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
1.000064 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003695_03054.