Species | UMGS1603 sp900553265 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1603; UMGS1603 sp900553265 | |||||||||||
CAZyme ID | MGYG000001823_01076 | |||||||||||
CAZy Family | GH95 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 33658; End: 35385 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH95 | 71 | 550 | 1e-112 | 0.6329639889196675 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1554 | ATH1 | 0.002 | 246 | 358 | 443 | 548 | Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism]. |
pfam03632 | Glyco_hydro_65m | 0.005 | 246 | 358 | 125 | 229 | Glycosyl hydrolase family 65 central catalytic 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. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNF27939.1 | 3.53e-170 | 74 | 555 | 273 | 757 |
ACX62422.1 | 4.64e-170 | 71 | 559 | 277 | 770 |
AYB47098.1 | 9.57e-168 | 73 | 557 | 297 | 787 |
QKS45791.1 | 1.09e-166 | 3 | 555 | 149 | 758 |
QZN78893.1 | 5.85e-166 | 74 | 559 | 303 | 793 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2RDY_A | 2.30e-38 | 78 | 531 | 281 | 732 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
4UFC_A | 6.09e-37 | 127 | 531 | 332 | 721 | Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus] |
7KMQ_A | 2.73e-34 | 3 | 552 | 235 | 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] |
2EAB_A | 1.64e-17 | 127 | 517 | 375 | 814 | 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 | 2.17e-17 | 127 | 517 | 375 | 814 | 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 | 1.02e-44 | 78 | 531 | 337 | 792 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000026 | 0.000021 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.