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CAZyme Information: EPrPVT00000019673-p1

You are here: Home > Sequence: EPrPVT00000019673-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Phytopythium vexans
Lineage Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
CAZyme ID EPrPVT00000019673-p1
CAZy Family GH43
CAZyme Description Chitobiosyldiphosphodolichol beta-mannosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
437 48794.09 10.1279
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PvexansDAOMBR484 11991 1223560 34 11957
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.142:10 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT33 145 429 1e-102 0.6517647058823529

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
340843 GT33_ALG1-like 5.63e-154 20 431 4 411
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins. This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.
215155 PLN02275 2.74e-144 20 396 5 371
transferase, transferring glycosyl groups
223515 RfaB 1.57e-10 66 397 36 341
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340831 GT4_PimA-like 1.79e-09 24 425 2 363
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.
340816 Glycosyltransferase_GTB-type 3.60e-07 251 382 114 235
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.33e-203 19 437 80 565
3.35e-146 21 430 11 446
3.91e-122 22 430 8 455
3.91e-122 22 430 8 455
2.77e-121 22 437 8 462

PDB Hits      help

EPrPVT00000019673-p1 has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.94e-117 22 430 7 454
UDP-glycosyltransferase TURAN OS=Arabidopsis thaliana OX=3702 GN=TUN PE=2 SV=1
4.07e-101 2 430 25 460
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Pongo abelii OX=9601 GN=ALG1 PE=2 SV=1
1.15e-100 16 430 29 460
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Homo sapiens OX=9606 GN=ALG1 PE=1 SV=2
1.93e-97 19 430 32 460
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Mus musculus OX=10090 GN=Alg1 PE=1 SV=3
3.67e-76 24 431 6 462
Chitobiosyldiphosphodolichol beta-mannosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000046 0.000002

TMHMM  Annotations      download full data without filtering help

Start End
90 112