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CAZyme Information: MGYG000004461_02199

You are here: Home > Sequence: MGYG000004461_02199

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
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; ;
CAZyme ID MGYG000004461_02199
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
429 49777.58 6.5045
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004461 4658877 MAG Israel Asia
Gene Location Start: 81311;  End: 82600  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004461_02199.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 20 312 1.3e-77 0.8901734104046243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00812 Alpha_L_fucos 4.63e-83 27 346 23 372
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 3.50e-73 27 303 22 328
Alpha-L-fucosidase.
COG3669 AfuC 1.67e-33 67 406 45 421
Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QHS63289.1 8.24e-127 19 425 25 426
ACU60079.1 3.77e-125 19 425 25 426
ACT91401.1 1.67e-124 19 426 25 429
QNN24421.1 4.17e-122 19 426 29 431
QRR03212.1 4.47e-122 19 406 26 410

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6GN6_A 4.65e-50 23 346 30 380
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]
1ODU_A 6.76e-33 27 380 24 408
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]
2WSP_A 6.76e-33 27 380 24 408
Thermotogamaritima alpha-L-fucosynthase, TmD224G, in complex with alpha-L-Fuc-(1-2)-beta-L-Fuc-N3 [Thermotoga maritima MSB8],2WSP_B Thermotoga maritima alpha-L-fucosynthase, TmD224G, in complex with alpha-L-Fuc-(1-2)-beta-L-Fuc-N3 [Thermotoga maritima MSB8]
2ZWY_A 7.32e-33 27 380 24 408
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 1.11e-32 14 382 9 410
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 3.46e-27 27 345 44 394
Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q5RFI5 4.95e-25 9 375 30 424
Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1
Q9BTY2 9.27e-25 9 382 32 444
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q6AYS4 3.99e-24 27 345 42 392
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
P49713 2.40e-22 27 332 34 369
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004461_02199.