Species | Cryptococcus cf. gattii | |||||||||||
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Lineage | Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus cf. gattii | |||||||||||
CAZyme ID | KAE8541590.1 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.4.1.231:3 |
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Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
340823 | GT4_trehalose_phosphorylase | 2.32e-172 | 234 | 650 | 1 | 378 | trehalose phosphorylase and similar proteins. Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases. |
223515 | RfaB | 7.77e-17 | 231 | 613 | 1 | 339 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
395425 | Glycos_transf_1 | 3.39e-14 | 451 | 622 | 1 | 150 | Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. |
404563 | Glyco_trans_1_4 | 1.08e-11 | 458 | 613 | 7 | 135 | Glycosyl transferases group 1. |
340816 | Glycosyltransferase_GTB-type | 5.54e-11 | 382 | 598 | 52 | 235 | glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 735 | 1 | 734 | |
0.0 | 1 | 735 | 1 | 734 | |
0.0 | 1 | 735 | 1 | 734 | |
0.0 | 1 | 735 | 1 | 734 | |
0.0 | 1 | 735 | 1 | 734 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.50e-35 | 234 | 619 | 42 | 383 | Crystal structure of trehalose synthase TreT from P.horikoshi [Pyrococcus horikoshii],2X6Q_B Crystal structure of trehalose synthase TreT from P.horikoshi [Pyrococcus horikoshii],2X6R_A Crystal structure of trehalose synthase TreT from P.horikoshi produced by soaking in trehalose [Pyrococcus horikoshii],2X6R_B Crystal structure of trehalose synthase TreT from P.horikoshi produced by soaking in trehalose [Pyrococcus horikoshii] |
|
9.31e-35 | 234 | 619 | 42 | 383 | Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XA2_B Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XA9_A Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XA9_B Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XMP_A Crystal structure of trehalose synthase TreT mutant E326A from P. horishiki in complex with UDP [Pyrococcus horikoshii],2XMP_B Crystal structure of trehalose synthase TreT mutant E326A from P. horishiki in complex with UDP [Pyrococcus horikoshii] |
|
1.26e-34 | 234 | 619 | 42 | 383 | Crystal structure of trehalose synthase TreT from P.horikoshii (Seleno derivative) [Pyrococcus horikoshii],2XA1_B Crystal structure of trehalose synthase TreT from P.horikoshii (Seleno derivative) [Pyrococcus horikoshii] |
|
2.04e-30 | 233 | 605 | 27 | 351 | Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis],6ZJ7_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis 768-20],6ZJH_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis 768-20],6ZMZ_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis],6ZN1_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.21e-97 | 193 | 677 | 236 | 694 | Trehalose phosphorylase OS=Pleurotus pulmonarius OX=28995 GN=TP PE=2 SV=1 |
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1.11e-95 | 3 | 677 | 11 | 686 | Trehalose phosphorylase OS=Grifola frondosa OX=5627 PE=1 SV=1 |
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1.34e-92 | 193 | 677 | 236 | 706 | Trehalose phosphorylase OS=Pleurotus sajor-caju OX=50053 GN=TP PE=1 SV=1 |
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5.38e-37 | 229 | 644 | 35 | 397 | Trehalose synthase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=treT PE=1 SV=1 |
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5.38e-37 | 229 | 644 | 35 | 397 | Trehalose synthase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=treT PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000040 | 0.000002 |
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