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CAZyme Information: MGYG000002662_00843

You are here: Home > Sequence: MGYG000002662_00843

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 UBA3388 sp900546465
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; P3; UBA3388; UBA3388 sp900546465
CAZyme ID MGYG000002662_00843
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
583 67694.5 5.6058
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002662 2000155 MAG United Republic of Tanzania Africa
Gene Location Start: 51235;  End: 52986  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002662_00843.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 15 350 7.6e-92 0.930635838150289

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00812 Alpha_L_fucos 2.59e-110 25 361 12 349
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 1.80e-109 17 347 3 333
Alpha-L-fucosidase.
COG3669 AfuC 2.43e-47 46 351 1 321
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
smart00758 PA14 5.17e-10 373 480 26 133
domain in bacterial beta-glucosidases other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins.
pfam07691 PA14 1.17e-09 368 473 23 130
PA14 domain. This domain forms an insert in bacterial beta-glucosidases and is found in other glycosidases, glycosyltransferases, proteases, amidases, yeast adhesins, and bacterial toxins, including anthrax protective antigen (PA). The domain also occurs in a Dictyostelium prespore-cell-inducing factor Psi and in fibrocystin, the mammalian protein whose mutation leads to polycystic kidney and hepatic disease. The crystal structure of PA shows that this domain (named PA14 after its location in the PA20 pro-peptide) has a beta-barrel structure. The PA14 domain sequence suggests a binding function, rather than a catalytic role. The PA14 domain distribution is compatible with carbohydrate binding.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QZE15454.1 1.27e-178 1 581 1 609
QCX39739.1 2.05e-177 1 576 13 608
APS38947.1 5.47e-170 1 577 1 591
QIK54993.1 1.47e-169 6 576 9 598
QIK60426.1 2.95e-169 6 576 9 598

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1ODU_A 7.37e-71 25 372 13 379
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 8.62e-71 25 372 13 379
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]
1HL8_A 1.44e-70 25 372 13 379
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]
2WSP_A 7.76e-70 25 372 13 379
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]
7LJJ_A 2.32e-45 20 369 44 419
ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P10901 1.01e-76 5 363 6 374
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
Q99KR8 1.22e-73 23 361 31 373
Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
C3YWU0 6.70e-73 5 392 3 401
Alpha-L-fucosidase OS=Branchiostoma floridae OX=7739 GN=BRAFLDRAFT_56888 PE=3 SV=2
Q9VTJ4 7.84e-73 27 361 41 379
Putative alpha-L-fucosidase OS=Drosophila melanogaster OX=7227 GN=Fuca PE=2 SV=2
Q5RFI5 3.93e-72 23 361 35 377
Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 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
0.000690 0.998330 0.000275 0.000262 0.000230 0.000207

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002662_00843.