Species | Bacteroides cellulosilyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides cellulosilyticus | |||||||||||
CAZyme ID | MGYG000002455_00431 | |||||||||||
CAZy Family | GH95 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 31912; End: 34383 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH95 | 24 | 760 | 3.4e-290 | 0.9861495844875346 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam14498 | Glyco_hyd_65N_2 | 3.47e-84 | 29 | 263 | 1 | 231 | Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain. |
PRK13807 | PRK13807 | 3.41e-04 | 135 | 301 | 106 | 301 | maltose phosphorylase; Provisional |
pfam03636 | Glyco_hydro_65N | 0.002 | 136 | 229 | 91 | 199 | Glycosyl hydrolase family 65, N-terminal domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity although its precise function remains unknown. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT89413.1 | 0.0 | 1 | 823 | 1 | 823 |
ALJ59551.1 | 0.0 | 1 | 823 | 1 | 823 |
AII65975.1 | 0.0 | 1 | 819 | 1 | 819 |
AND19242.1 | 0.0 | 1 | 819 | 1 | 819 |
QUT86309.1 | 0.0 | 1 | 819 | 1 | 819 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4UFC_A | 4.04e-272 | 3 | 822 | 4 | 807 | Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus] |
7KMQ_A | 5.13e-218 | 17 | 755 | 31 | 757 | ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306] |
2RDY_A | 4.19e-186 | 31 | 748 | 7 | 745 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
2EAB_A | 2.42e-90 | 29 | 775 | 20 | 880 | Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum] |
2EAD_A | 6.43e-90 | 29 | 775 | 20 | 880 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8L7W8 | 3.22e-156 | 29 | 740 | 54 | 797 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
A2R797 | 2.10e-100 | 14 | 740 | 8 | 761 | Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1 |
Q5AU81 | 2.34e-87 | 44 | 730 | 46 | 771 | Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1 |
Q2USL3 | 5.48e-60 | 29 | 757 | 18 | 714 | Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000315 | 0.998935 | 0.000256 | 0.000153 | 0.000152 | 0.000140 |
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