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CAZyme Information: MGYG000000658_00539

You are here: Home > Sequence: MGYG000000658_00539

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; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia;
CAZyme ID MGYG000000658_00539
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
765 MGYG000000658_3|CGC1 85450.03 5.9957
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000658 1755704 MAG Germany Europe
Gene Location Start: 82550;  End: 84847  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000658_00539.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 85 418 7e-72 0.8294797687861272
CBM32 642 762 2.6e-19 0.8951612903225806

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 2.72e-52 69 531 2 424
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 2.01e-31 119 418 85 326
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 5.26e-29 119 418 82 328
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.
pfam00754 F5_F8_type_C 1.19e-18 650 762 14 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam13290 CHB_HEX_C_1 8.11e-10 579 619 18 59
Chitobiase/beta-hexosaminidase C-terminal domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRO25056.1 0.0 46 764 32 749
QTO26413.1 0.0 25 764 3 736
QCQ30568.1 0.0 25 764 3 736
QUT50205.1 0.0 45 764 20 712
ASO05171.1 0.0 34 763 8 743

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 2.73e-109 47 748 4 566
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
3UES_A 6.70e-100 72 536 16 475
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 1.96e-99 72 536 18 477
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]
3UET_A 7.67e-98 72 536 16 475
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UET_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3EYP_A 8.11e-77 73 531 8 448
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GW72 5.52e-80 74 553 37 498
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.61e-71 74 531 39 470
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P10901 1.39e-08 111 417 98 350
Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
Q9BTY2 3.26e-08 95 261 95 229
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q5RFI5 4.29e-08 95 417 93 355
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
0.128512 0.848543 0.021425 0.000863 0.000347 0.000303

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000658_00539.