Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; ; | |||||||||||
CAZyme ID | MGYG000000390_01880 | |||||||||||
CAZy Family | CBM57 | |||||||||||
CAZyme Description | Beta-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 14; End: 2425 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM57 | 634 | 798 | 5.8e-42 | 0.9863945578231292 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam11721 | Malectin | 2.25e-30 | 632 | 801 | 1 | 156 | Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan. |
COG3250 | LacZ | 1.87e-16 | 228 | 342 | 291 | 407 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam02836 | Glyco_hydro_2_C | 6.52e-14 | 227 | 379 | 5 | 167 | Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
PRK10150 | PRK10150 | 2.00e-11 | 198 | 373 | 257 | 449 | beta-D-glucuronidase; Provisional |
pfam16355 | DUF4982 | 2.25e-09 | 544 | 600 | 8 | 62 | Domain of unknown function (DUF4982). This family is found in the C-terminal of uncharacterized proteins and beta-galactosidases around 680 residues in length from various Bacteroides species. The function of this protein is unknown. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALJ01732.1 | 1.26e-239 | 226 | 801 | 329 | 900 |
QHJ06763.1 | 2.99e-232 | 226 | 801 | 327 | 899 |
ACU05015.1 | 1.41e-231 | 229 | 801 | 326 | 893 |
QEC55690.1 | 1.24e-226 | 229 | 801 | 407 | 974 |
QTE40581.1 | 2.49e-225 | 228 | 801 | 367 | 933 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6D1P_A | 4.14e-36 | 227 | 646 | 313 | 745 | Apostructure of Bacteroides uniformis beta-glucuronidase 3 [Bacteroides uniformis str. 3978 T3 ii],6D1P_B Apo structure of Bacteroides uniformis beta-glucuronidase 3 [Bacteroides uniformis str. 3978 T3 ii] |
6D7J_A | 1.39e-30 | 227 | 590 | 315 | 700 | TheCrystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) with Glycerol in Active-Site [Parabacteroides merdae CL03T12C32],6D7J_B The Crystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) with Glycerol in Active-Site [Parabacteroides merdae CL03T12C32],6D7J_C The Crystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) with Glycerol in Active-Site [Parabacteroides merdae CL03T12C32],6D7J_D The Crystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) with Glycerol in Active-Site [Parabacteroides merdae CL03T12C32],6DXU_A Crystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) [Parabacteroides merdae ATCC 43184],6DXU_B Crystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) [Parabacteroides merdae ATCC 43184],6DXU_C Crystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) [Parabacteroides merdae ATCC 43184],6DXU_D Crystal Structure of Parabacteroides merdae Beta-Glucuronidase (GUS) [Parabacteroides merdae ATCC 43184] |
5UJ6_A | 7.04e-28 | 226 | 770 | 302 | 845 | CrystalStructure of Bacteroides Uniformis beta-glucuronidase [Bacteroides uniformis str. 3978 T3 ii],5UJ6_B Crystal Structure of Bacteroides Uniformis beta-glucuronidase [Bacteroides uniformis str. 3978 T3 ii],6NZG_A Bacteroides uniformis beta-glucuronidase 2 covalently bound to cyclophellitol-6-carboxylate aziridine [Bacteroides uniformis],6NZG_B Bacteroides uniformis beta-glucuronidase 2 covalently bound to cyclophellitol-6-carboxylate aziridine [Bacteroides uniformis] |
6D50_A | 7.12e-28 | 226 | 770 | 310 | 853 | Bacteroidesuniforms beta-glucuronidase 2 bound to D-glucaro-1,5-lactone [Bacteroides uniformis str. 3978 T3 ii],6D50_B Bacteroides uniforms beta-glucuronidase 2 bound to D-glucaro-1,5-lactone [Bacteroides uniformis str. 3978 T3 ii] |
6D8G_A | 1.24e-27 | 226 | 770 | 310 | 853 | D341AD367A calcium binding mutant of Bacteroides uniformis beta-glucuronidase 2 [Bacteroides uniformis str. 3978 T3 ii],6D8G_B D341A D367A calcium binding mutant of Bacteroides uniformis beta-glucuronidase 2 [Bacteroides uniformis str. 3978 T3 ii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
T2KPJ7 | 3.00e-34 | 230 | 603 | 318 | 718 | Putative beta-glucuronidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_21970 PE=2 SV=1 |
O77695 | 6.16e-14 | 227 | 513 | 330 | 623 | Beta-glucuronidase (Fragment) OS=Chlorocebus aethiops OX=9534 GN=GUSB PE=2 SV=1 |
Q4FAT7 | 1.70e-12 | 227 | 513 | 333 | 626 | Beta-glucuronidase OS=Sus scrofa OX=9823 GN=GUSB PE=3 SV=1 |
P08236 | 2.24e-12 | 227 | 513 | 333 | 626 | Beta-glucuronidase OS=Homo sapiens OX=9606 GN=GUSB PE=1 SV=2 |
O18835 | 6.76e-12 | 227 | 513 | 332 | 625 | Beta-glucuronidase OS=Canis lupus familiaris OX=9615 GN=GUSB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000030 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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