Species | Kwoniella mangrovensis | |||||||||||
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Lineage | Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella mangrovensis | |||||||||||
CAZyme ID | OCF64286.1 | |||||||||||
CAZy Family | GH128 | |||||||||||
CAZyme Description | phosphatidylinositol glycan, class A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.4.1.198:3 |
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Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
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340827 | GT4_PIG-A-like | 0.0 | 346 | 745 | 1 | 398 | phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder. |
340831 | GT4_PimA-like | 2.35e-57 | 347 | 713 | 2 | 366 | 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. |
153251 | LPLAT_AGPAT-like | 2.96e-50 | 55 | 244 | 7 | 184 | Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins. |
223515 | RfaB | 6.64e-47 | 347 | 717 | 3 | 379 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
223282 | PlsC | 6.30e-42 | 11 | 251 | 3 | 227 | 1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 783 | 1 | 789 | |
0.0 | 1 | 777 | 1 | 775 | |
0.0 | 1 | 777 | 1 | 775 | |
0.0 | 1 | 777 | 1 | 775 | |
0.0 | 1 | 784 | 1 | 726 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.68e-22 | 82 | 252 | 74 | 242 | Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima [Thermotoga maritima MSB8],5KYM_B Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima [Thermotoga maritima MSB8] |
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3.64e-13 | 345 | 714 | 15 | 398 | Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155] |
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1.35e-10 | 345 | 713 | 5 | 365 | Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_A Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_B Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_C Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_D Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155] |
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1.45e-10 | 345 | 713 | 21 | 381 | Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man [Mycolicibacterium smegmatis MC2 155],2GEK_A Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP [Mycolicibacterium smegmatis MC2 155] |
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5.66e-10 | 356 | 655 | 24 | 323 | 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 |
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6.59e-145 | 349 | 765 | 1 | 415 | Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gpi3 PE=3 SV=1 |
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4.76e-131 | 346 | 766 | 34 | 454 | Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Mus musculus OX=10090 GN=Piga PE=2 SV=1 |
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5.08e-130 | 346 | 766 | 34 | 453 | Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Homo sapiens OX=9606 GN=PIGA PE=1 SV=1 |
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1.46e-127 | 344 | 765 | 6 | 423 | Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Arabidopsis thaliana OX=3702 GN=PIGA PE=2 SV=1 |
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6.76e-112 | 346 | 766 | 4 | 433 | Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit OS=Saccharomyces cerevisiae (strain RM11-1a) OX=285006 GN=SPT14 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000054 | 0.000001 |
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