Species | Enterococcus_D casseliflavus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_D; Enterococcus_D casseliflavus | |||||||||||
CAZyme ID | MGYG000000238_01345 | |||||||||||
CAZy Family | GH65 | |||||||||||
CAZyme Description | Alpha,alpha-trehalose phosphorylase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 103330; End: 105456 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH65 | 287 | 649 | 5.1e-136 | 0.9946236559139785 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1554 | ATH1 | 1.76e-178 | 5 | 679 | 9 | 733 | Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism]. |
pfam03632 | Glyco_hydro_65m | 5.63e-126 | 287 | 650 | 1 | 385 | 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. |
PRK13807 | PRK13807 | 9.23e-125 | 5 | 678 | 8 | 721 | maltose phosphorylase; Provisional |
pfam03636 | Glyco_hydro_65N | 3.96e-31 | 12 | 164 | 3 | 149 | 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 |
---|---|---|---|---|---|
QOG31903.1 | 0.0 | 1 | 708 | 1 | 708 |
AMG48503.1 | 0.0 | 1 | 708 | 1 | 708 |
AUJ86598.1 | 0.0 | 1 | 708 | 1 | 708 |
QOG28282.1 | 0.0 | 7 | 707 | 5 | 702 |
QCT90631.1 | 0.0 | 7 | 707 | 5 | 702 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3WIQ_A | 2.98e-96 | 23 | 701 | 22 | 751 | Crystalstructure of kojibiose phosphorylase complexed with kojibiose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_A Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_B Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_C Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_D Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903] |
1H54_A | 1.62e-85 | 23 | 679 | 26 | 724 | ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis] |
4KTP_A | 1.24e-60 | 26 | 700 | 33 | 736 | ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTP_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10] |
4KTR_A | 1.71e-60 | 26 | 700 | 33 | 736 | ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_C Chain C, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_D Chain D, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_E Chain E, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_F Chain F, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_G Chain G, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_H Chain H, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10] |
7FE3_A | 8.52e-45 | 257 | 667 | 277 | 665 | ChainA, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_A Chain A, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8L164 | 1.10e-166 | 5 | 690 | 13 | 753 | Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1 |
Q8GRC3 | 4.64e-163 | 6 | 679 | 2 | 723 | Alpha,alpha-trehalose phosphorylase OS=Geobacillus stearothermophilus OX=1422 GN=treP PE=1 SV=1 |
P9WN12 | 1.44e-119 | 23 | 672 | 28 | 715 | Uncharacterized glycosyl hydrolase MT3509 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3509 PE=3 SV=1 |
P9WN13 | 1.44e-119 | 23 | 672 | 28 | 715 | Uncharacterized glycosyl hydrolase Rv3401 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3401 PE=1 SV=1 |
Q49736 | 4.32e-115 | 23 | 672 | 28 | 715 | Uncharacterized glycosyl hydrolase ML0392 OS=Mycobacterium leprae (strain TN) OX=272631 GN=ML0392 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000069 | 0.000000 | 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.