Species | Exophiala mesophila | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila | |||||||||||
CAZyme ID | PV10_03549-t45_2-p1 | |||||||||||
CAZy Family | GH16 | |||||||||||
CAZyme Description | hypothetical protein, variant | |||||||||||
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 | 1.84e-161 | 35 | 454 | 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 | 5.03e-22 | 32 | 437 | 1 | 360 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
395425 | Glycos_transf_1 | 2.72e-20 | 262 | 433 | 4 | 158 | 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. |
340831 | GT4_PimA-like | 8.72e-18 | 36 | 436 | 5 | 350 | phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the 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. The members of this family are found mainly in certain bacteria and archaea. |
340828 | GT4_WlbH-like | 6.93e-15 | 249 | 441 | 188 | 372 | Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
6.94e-210 | 2 | 490 | 188 | 677 | |
9.99e-210 | 2 | 490 | 199 | 688 | |
9.99e-210 | 2 | 490 | 199 | 688 | |
9.99e-210 | 2 | 490 | 199 | 688 | |
9.99e-210 | 2 | 490 | 199 | 688 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.21e-37 | 7 | 456 | 16 | 416 | 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] |
|
8.28e-37 | 7 | 456 | 16 | 416 | 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] |
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2.03e-35 | 7 | 456 | 16 | 416 | 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] |
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3.17e-32 | 7 | 434 | 2 | 375 | 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] |
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2.60e-09 | 238 | 437 | 193 | 368 | Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_B Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_C Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_D Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_E Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_F Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_G Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_H Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_I Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_J Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_K Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_L Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.01e-196 | 7 | 488 | 246 | 725 | Trehalose phosphorylase OS=Grifola frondosa OX=5627 PE=1 SV=1 |
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3.03e-195 | 7 | 488 | 250 | 732 | Trehalose phosphorylase OS=Pleurotus pulmonarius OX=28995 GN=TP PE=2 SV=1 |
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3.57e-186 | 7 | 488 | 250 | 744 | Trehalose phosphorylase OS=Pleurotus sajor-caju OX=50053 GN=TP PE=1 SV=1 |
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3.61e-43 | 7 | 453 | 14 | 411 | 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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3.61e-43 | 7 | 453 | 14 | 411 | 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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1.000071 | 0.000000 |
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