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CAZyme Information: PV10_05786-t45_1-p1

You are here: Home > Sequence: PV10_05786-t45_1-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 Exophiala mesophila
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
CAZyme ID PV10_05786-t45_1-p1
CAZy Family GH72
CAZyme Description hypothetical protein, variant
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
727 KN847523|CGC7 80906.64 5.3319
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EmesophilaCBS40295 9237 N/A 56 9181
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.186:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT8 9 220 1.6e-42 0.867704280155642

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
133018 GT8_Glycogenin 8.35e-84 8 246 2 240
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen. Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.
279798 Glyco_transf_8 5.41e-25 11 219 3 248
Glycosyl transferase family 8. This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.
132996 Glyco_transf_8 1.13e-22 9 219 3 244
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.
133037 GT8_A4GalT_like 4.55e-21 8 219 4 246
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.
224359 RfaJ 3.38e-19 97 259 96 283
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.03e-184 5 614 5 660
3.13e-176 7 614 6 750
8.74e-176 1 615 1 681
3.02e-173 5 614 4 749
3.62e-170 7 614 7 709

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.37e-50 9 249 7 260
Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP, in a triclinic closed form [Homo sapiens],3T7M_B Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP, in a triclinic closed form [Homo sapiens],3T7N_A Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP, in a monoclinic closed form [Homo sapiens],3T7N_B Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP, in a monoclinic closed form [Homo sapiens],3T7O_A Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP-Glucose and glucose [Homo sapiens],3T7O_B Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP-Glucose and glucose [Homo sapiens],3U2U_A Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and maltotetraose [Homo sapiens],3U2U_B Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and maltotetraose [Homo sapiens],3U2V_A Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and maltohexaose [Homo sapiens],3U2V_B Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and maltohexaose [Homo sapiens],3U2X_A Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and 1'-deoxyglucose [Homo sapiens],3U2X_B Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and 1'-deoxyglucose [Homo sapiens]
9.76e-50 9 249 28 281
Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese [Homo sapiens]
1.95e-49 9 249 7 260
Crystal Structure of Human Glycogenin-1 (GYG1), apo form [Homo sapiens],3QVB_A Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP [Homo sapiens],3U2W_A Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and glucose or a glucal species [Homo sapiens],3U2W_B Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and glucose or a glucal species [Homo sapiens]
3.72e-49 9 249 7 260
Crystal Structure of Human Glycogenin-1 (GYG1) T83M mutant complexed with manganese and UDP [Homo sapiens],3RMW_A Crystal Structure of Human Glycogenin-1 (GYG1) T83M mutant complexed with manganese and UDP-glucose [Homo sapiens]
7.10e-49 9 249 7 260
Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant, apo form [Homo sapiens],6EQL_A Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant complexed with manganese and UDP [Homo sapiens],6EQL_B Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant complexed with manganese and UDP [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.23e-49 9 249 6 259
Glycogenin-1 OS=Mus musculus OX=10090 GN=Gyg1 PE=1 SV=3
2.92e-48 9 249 6 259
Glycogenin-1 OS=Homo sapiens OX=9606 GN=GYG1 PE=1 SV=4
1.29e-47 9 243 6 253
Glycogenin-1 OS=Oryctolagus cuniculus OX=9986 GN=GYG1 PE=1 SV=3
2.30e-46 9 249 6 259
Glycogenin-1 OS=Rattus norvegicus OX=10116 GN=Gyg1 PE=2 SV=4
6.14e-46 11 246 7 241
Glycogenin-1 OS=Caenorhabditis elegans OX=6239 GN=gyg-1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.980395 0.019626

TMHMM  Annotations      help

There is no transmembrane helices in PV10_05786-t45_1-p1.