Species | Collinsella sp900556495 | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900556495 | |||||||||||
CAZyme ID | MGYG000003361_00054 | |||||||||||
CAZy Family | GH29 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 57845; End: 62005 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH29 | 42 | 382 | 1.4e-55 | 0.8901734104046243 |
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. |
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 |
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] |
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 |
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 |
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