Species | UBA6398 sp900550635 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; UBA6398; UBA6398 sp900550635 | |||||||||||
CAZyme ID | MGYG000001058_01008 | |||||||||||
CAZy Family | GH65 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 7316; End: 9346 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH65 | 302 | 640 | 9.7e-98 | 0.9946236559139785 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1554 | ATH1 | 9.30e-99 | 40 | 660 | 31 | 721 | Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism]. |
pfam03632 | Glyco_hydro_65m | 6.89e-64 | 302 | 640 | 1 | 384 | 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 | 1.51e-45 | 71 | 660 | 75 | 710 | maltose phosphorylase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AUP80081.1 | 1.53e-253 | 1 | 670 | 1 | 671 |
AWX45602.1 | 1.08e-249 | 22 | 672 | 21 | 678 |
AXT56849.1 | 6.87e-247 | 2 | 669 | 8 | 680 |
BAX82702.1 | 5.19e-245 | 15 | 669 | 19 | 674 |
SDS46993.1 | 1.76e-243 | 1 | 669 | 1 | 674 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7FE3_A | 5.69e-191 | 24 | 669 | 22 | 674 | 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] |
3WIQ_A | 4.82e-50 | 227 | 657 | 230 | 714 | 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 | 1.51e-34 | 71 | 666 | 75 | 718 | ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis] |
4KTP_A | 4.73e-30 | 227 | 662 | 225 | 714 | 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 | 8.35e-30 | 227 | 662 | 225 | 714 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q54KX5 | 5.22e-71 | 271 | 643 | 252 | 632 | Protein-glucosylgalactosylhydroxylysine glucosidase OS=Dictyostelium discoideum OX=44689 GN=pgghg PE=3 SV=2 |
Q8L163 | 1.89e-55 | 269 | 660 | 292 | 735 | Kojibiose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=kojP PE=1 SV=1 |
A0JMP0 | 1.58e-53 | 277 | 662 | 186 | 585 | Protein-glucosylgalactosylhydroxylysine glucosidase OS=Danio rerio OX=7955 GN=pgghg PE=2 SV=1 |
Q8BP56 | 4.36e-52 | 277 | 643 | 230 | 608 | Protein-glucosylgalactosylhydroxylysine glucosidase OS=Mus musculus OX=10090 GN=Pgghg PE=1 SV=1 |
Q32M88 | 3.63e-51 | 257 | 643 | 210 | 609 | Protein-glucosylgalactosylhydroxylysine glucosidase OS=Homo sapiens OX=9606 GN=PGGHG PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000289 | 0.998931 | 0.000222 | 0.000179 | 0.000175 | 0.000172 |
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