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CAZyme Information: NEUDI_58245T0-p1

You are here: Home > Sequence: NEUDI_58245T0-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 Neurospora discreta
Lineage Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
CAZyme ID NEUDI_58245T0-p1
CAZy Family GH55
CAZyme Description Glycosyl transferase, family 8 - glycogenin
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
311 NdisFGSC8579_SC005|CGC4 35402.59 7.1882
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_NdiscretaFGSC8579 10345 510953 397 9948
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in NEUDI_58245T0-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT8 13 260 1.8e-39 0.8638132295719845

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
133018 GT8_Glycogenin 2.21e-71 9 282 1 239
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.
215090 PLN00176 1.08e-16 20 282 35 293
galactinol synthase
279798 Glyco_transf_8 3.52e-11 20 258 10 248
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.
133037 GT8_A4GalT_like 2.62e-10 94 258 95 246
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.
133064 GT8_GNT1 1.49e-09 11 196 3 150
GNT1 is a fungal enzyme that belongs to the GT 8 family. N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.76e-73 2 290 4 295
9.38e-70 5 291 4 305
6.37e-69 11 288 9 289
3.97e-68 1 285 1 299
3.16e-67 1 285 1 299

PDB Hits      help

NEUDI_58245T0-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
3.65e-17 20 295 35 308
Galactinol synthase 1 OS=Ajuga reptans OX=38596 GN=GOLS1 PE=1 SV=1
1.28e-16 20 278 28 283
Galactinol synthase 3 OS=Arabidopsis thaliana OX=3702 GN=GOLS3 PE=1 SV=1
2.84e-15 20 298 34 309
Galactinol synthase 2 OS=Arabidopsis thaliana OX=3702 GN=GOLS2 PE=1 SV=1
3.03e-14 31 267 7 240
Galactinol synthase 2 (Fragment) OS=Ajuga reptans OX=38596 GN=GOLS2 PE=1 SV=1
3.32e-14 14 311 31 325
Galactinol synthase 6 OS=Arabidopsis thaliana OX=3702 GN=GOLS6 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000062 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in NEUDI_58245T0-p1.