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CAZyme Information: MGYG000003361_00054

You are here: Home > Sequence: MGYG000003361_00054

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 Collinsella sp900556495
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900556495
CAZyme ID MGYG000003361_00054
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1386 147231.95 4.6868
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003361 2140862 MAG United States North America
Gene Location Start: 57845;  End: 62005  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003361_00054.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 42 382 1.4e-55 0.8901734104046243

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 4.45e-57 49 528 11 430
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
smart00812 Alpha_L_fucos 1.96e-21 56 378 23 327
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 1.68e-19 94 379 82 326
Alpha-L-fucosidase.
cd04080 CBM6_cellulase-like 5.93e-09 848 968 3 129
Carbohydrate Binding Module 6 (CBM6); appended to glycoside hydrolase (GH) domains, including GH5 (cellulase). This family includes carbohydrate binding module 6 (CBM6) domains that are appended to several glycoside hydrolase (GH) domains, including GH5 (cellulase) and GH16, as well as to coagulation factor 5/8 carbohydrate-binding domains. CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. The CBM6s are appended to GHs that display a diversity of substrate specificities. For some members of this family information is available about the specific substrates of the appended GH domains. It includes the CBM domains of various enzymes involved in cell wall degradation including, an extracellular beta-1,3-glucanase from Lysobacter enzymogenes encoded by the gluC gene (its catalytic domain belongs to the GH16 family), the tandem CBM domains of Pseudomonas sp. PE2 beta-1,3(4)-glucanase A (its catalytic domain also belongs to GH16), and a family 6 CBM from Cellvibrio mixtus Endoglucanase 5A (CmCBM6) which binds to the beta1,4-beta1,3-mixed linked glucans lichenan, and barley beta-glucan, cello-oligosaccharides, insoluble forms of cellulose, the beta1,3-glucan laminarin, and xylooligosaccharides, and the CBM6 of Fibrobacter succinogenes S85 XynD xylanase, appended to a GH10 domain, and Cellvibrio japonicas Cel5G appended to a GH5 (cellulase) domain. GH5 (cellulase) family includes enzymes with several known activities such as endoglucanase, beta-mannanase, and xylanase, which are involved in the degradation of cellulose and xylans. GH16 family includes enzymes with lichenase, xyloglucan endotransglycosylase (XET), and beta-agarase activities. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. For CmCBM6 it has been shown that these two binding sites have different ligand specificities.
pfam07554 FIVAR 1.72e-08 995 1054 2 68
FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QHB23055.1 4.21e-287 39 1255 56 1297
QEI30547.1 4.21e-287 39 1255 56 1297
QRT29448.1 4.32e-287 39 1255 56 1297
PLT74914.1 6.06e-278 39 1284 56 1322
QPK81604.1 1.25e-221 42 995 46 1013

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6TR3_A 9.03e-188 39 561 18 544
Ruminococcusgnavus GH29 fucosidase E1_10125 in complex with fucose [[Ruminococcus] gnavus E1]
6TR4_A 1.37e-186 39 561 18 544
Ruminococcusgnavus GH29 fucosidase E1_10125 D221A mutant in complex with fucose [[Ruminococcus] gnavus E1],6TR4_B Ruminococcus gnavus GH29 fucosidase E1_10125 D221A mutant in complex with fucose [[Ruminococcus] gnavus E1]
6ORG_A 3.94e-102 48 529 10 449
Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORG_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4]
6OR4_A 5.00e-101 48 529 10 449
Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6OR4_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORH_A Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORH_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4]
6ORF_A 5.16e-101 48 529 10 449
Crystalstructure of SpGH29 [Streptococcus pneumoniae TIGR4],6ORF_B Crystal structure of SpGH29 [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GW72 2.99e-73 48 528 37 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.80e-68 42 531 33 479
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713 1.38e-08 56 381 34 342
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q9BTY2 3.05e-08 56 382 78 361
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q5RFI5 9.19e-08 56 382 76 359
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
0.000349 0.998855 0.000160 0.000259 0.000184 0.000153

TMHMM  Annotations      download full data without filtering help

start end
12 34
1358 1380