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CAZyme Information: MGYG000001898_00802

You are here: Home > Sequence: MGYG000001898_00802

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 Parabacteroides sp900552415
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900552415
CAZyme ID MGYG000001898_00802
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
690 MGYG000001898_19|CGC1 77968.24 5.5642
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001898 3107743 MAG Denmark Europe
Gene Location Start: 658;  End: 2730  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001898_00802.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 40 343 9.3e-76 0.838150289017341

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 4.25e-59 28 472 1 418
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 4.46e-36 65 342 69 320
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 1.09e-34 65 345 66 325
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.
pfam13287 Fn3_assoc 1.77e-17 503 562 1 59
Fn3 associated.
pfam13290 CHB_HEX_C_1 1.70e-12 498 549 7 58
Chitobiase/beta-hexosaminidase C-terminal domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT97698.1 0.0 1 689 1 684
AST55451.1 0.0 1 689 1 684
QJE29484.1 0.0 1 689 1 684
QIX64728.1 0.0 1 689 1 684
QCY57860.1 0.0 1 689 1 684

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5K9H_A 1.10e-148 32 687 33 583
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
4ZRX_A 3.19e-116 37 671 31 566
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
3EYP_A 6.95e-114 37 474 9 444
Crystalstructure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],3EYP_B Crystal structure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],4OUE_A Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OUE_B Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_A Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_B Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482]
3UES_A 1.92e-105 38 473 19 465
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UES_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3MO4_A 6.19e-104 38 473 21 467
Thecrystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3MO4_B The crystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GW72 2.04e-102 31 467 31 460
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.80e-99 31 474 33 466
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713 6.23e-11 73 335 89 327
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
P10901 7.76e-11 49 335 80 338
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
Q9BTY2 1.83e-10 45 194 78 232
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 LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000030 1.000011 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001898_00802.