Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; | |||||||||||
CAZyme ID | MGYG000002717_02043 | |||||||||||
CAZy Family | GH51 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6074; End: 8602 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH51 | 385 | 725 | 1.7e-97 | 0.5047619047619047 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam06964 | Alpha-L-AF_C | 1.65e-38 | 653 | 830 | 1 | 192 | Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides. |
COG3534 | AbfA | 1.25e-36 | 388 | 836 | 32 | 498 | Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism]. |
smart00813 | Alpha-L-AF_C | 2.83e-31 | 653 | 830 | 1 | 189 | Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides. |
pfam02018 | CBM_4_9 | 2.90e-06 | 236 | 376 | 1 | 128 | Carbohydrate binding domain. This family includes diverse carbohydrate binding domains. |
cd18607 | GH130 | 0.006 | 43 | 151 | 29 | 128 | Glycoside hydrolase family 130. Members of the glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT89981.1 | 0.0 | 1 | 842 | 1 | 839 |
ALJ58903.1 | 0.0 | 1 | 842 | 1 | 839 |
QDO67474.1 | 0.0 | 1 | 842 | 1 | 840 |
AVM53995.1 | 0.0 | 1 | 842 | 1 | 839 |
BBK85669.1 | 0.0 | 1 | 842 | 1 | 846 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6ZPS_AAA | 1.57e-77 | 203 | 836 | 2 | 624 | ChainAAA, MgGH51 [Meripilus giganteus],6ZPV_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPW_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPX_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPY_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZPZ_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ0_AAA Chain AAA, MgGH51 [Meripilus giganteus],6ZQ1_AAA Chain AAA, MgGH51 [Meripilus giganteus] |
2VRQ_A | 1.30e-12 | 405 | 839 | 50 | 496 | StructureOf An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_B Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus],2VRQ_C Structure Of An Inactive Mutant Of Arabinofuranosidase From Thermobacillus Xylanilyticus In Complex With A Pentasaccharide [Thermobacillus xylanilyticus] |
6ZT6_A | 1.30e-12 | 405 | 839 | 50 | 496 | ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT6_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT7_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus] |
6ZTA_A | 1.30e-12 | 405 | 839 | 50 | 496 | ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZTA_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus] |
6ZT8_A | 2.27e-12 | 405 | 839 | 50 | 496 | ChainA, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT8_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_A Chain A, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_B Chain B, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus],6ZT9_C Chain C, Alpha-L-arabinofuranosidase [Thermobacillus xylanilyticus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P82593 | 5.95e-121 | 214 | 738 | 48 | 547 | Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 PE=1 SV=1 |
Q9SG80 | 9.23e-75 | 180 | 832 | 26 | 651 | Alpha-L-arabinofuranosidase 1 OS=Arabidopsis thaliana OX=3702 GN=ASD1 PE=1 SV=1 |
B8NKA3 | 6.93e-69 | 203 | 837 | 27 | 629 | Probable alpha-L-arabinofuranosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=abfA PE=3 SV=2 |
Q2U790 | 2.51e-68 | 203 | 837 | 27 | 629 | Probable alpha-L-arabinofuranosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=abfA PE=3 SV=2 |
Q8VZR2 | 1.16e-67 | 203 | 799 | 41 | 606 | Alpha-L-arabinofuranosidase 2 OS=Arabidopsis thaliana OX=3702 GN=ASD2 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000270 | 0.999027 | 0.000198 | 0.000167 | 0.000161 | 0.000144 |
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