Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; GCA-900066135; | |||||||||||
CAZyme ID | MGYG000004839_00405 | |||||||||||
CAZy Family | CBM57 | |||||||||||
CAZyme Description | Beta-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 62258; End: 65383 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM57 | 867 | 1037 | 2.9e-40 | 0.9863945578231292 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam11721 | Malectin | 1.66e-30 | 865 | 1037 | 1 | 164 | 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 | 1.72e-16 | 1 | 286 | 7 | 290 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
COG3250 | LacZ | 2.78e-14 | 333 | 582 | 174 | 413 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
pfam02837 | Glyco_hydro_2_N | 2.95e-14 | 8 | 165 | 3 | 168 | Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. |
pfam00703 | Glyco_hydro_2 | 6.97e-14 | 168 | 280 | 1 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEM17880.1 | 1.95e-258 | 4 | 1039 | 25 | 887 |
QEM05289.1 | 1.95e-258 | 4 | 1039 | 25 | 887 |
QTE40581.1 | 2.32e-258 | 4 | 1039 | 70 | 932 |
QTE57273.1 | 2.87e-258 | 4 | 1039 | 38 | 900 |
QTE45588.1 | 2.87e-258 | 4 | 1039 | 38 | 900 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5UJ6_A | 7.78e-39 | 4 | 1038 | 25 | 873 | 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 | 8.00e-39 | 4 | 1038 | 33 | 881 | 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] |
6D1P_A | 1.94e-34 | 405 | 836 | 276 | 704 | 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 | 3.55e-27 | 464 | 824 | 318 | 708 | 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] |
5T98_A | 6.06e-27 | 7 | 282 | 28 | 293 | Crystalstructure of BuGH2Awt [Bacteroides uniformis],5T98_B Crystal structure of BuGH2Awt [Bacteroides uniformis],5T99_A Crystal structure of BuGH2Awt in complex with Galactoisofagomine [Bacteroides uniformis],5T99_B Crystal structure of BuGH2Awt in complex with Galactoisofagomine [Bacteroides uniformis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
T2KPJ7 | 4.29e-37 | 3 | 838 | 52 | 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 |
T2KN75 | 1.14e-24 | 4 | 289 | 26 | 324 | Beta-glucuronidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22060 PE=1 SV=1 |
A7LXS9 | 1.91e-20 | 4 | 289 | 42 | 319 | Beta-galactosidase BoGH2A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02645 PE=1 SV=1 |
T2KM09 | 3.47e-19 | 4 | 289 | 46 | 314 | Putative beta-glucuronidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22050 PE=2 SV=2 |
P77989 | 1.89e-11 | 4 | 284 | 3 | 269 | Beta-galactosidase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=lacZ PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000071 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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