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CAZyme Information: MGYG000002797_00022

You are here: Home > Sequence: MGYG000002797_00022

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
Lineage Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; ;
CAZyme ID MGYG000002797_00022
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
495 56829.71 9.075
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002797 1235752 MAG United States North America
Gene Location Start: 72;  End: 1559  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002797_00022.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
NF033516 transpos_IS3 4.00e-73 251 482 135 368
IS3 family transposase.
cd04187 DPM1_like_bac 3.66e-48 1 138 46 181
Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.
PHA02517 PHA02517 3.02e-41 254 478 34 258
putative transposase OrfB; Reviewed
cd04179 DPM_DPG-synthase_like 2.91e-29 2 138 46 185
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.
COG2801 Tra5 7.51e-29 246 489 4 230
Transposase InsO and inactivated derivatives [Mobilome: prophages, transposons].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQP38874.1 1.77e-157 1 255 65 319
CBL39264.1 1.77e-157 1 255 65 319
BCD36661.1 1.76e-136 1 255 56 310
QMW70479.1 2.41e-136 1 255 65 319
BBF44274.1 2.63e-131 1 263 57 317

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5EKP_A 2.63e-47 15 255 89 329
Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa]
5EKE_A 3.75e-46 15 255 89 329
Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34755 9.74e-90 13 265 73 331
Uncharacterized glycosyltransferase YkoT OS=Bacillus subtilis (strain 168) OX=224308 GN=ykoT PE=1 SV=1
P57022 1.76e-54 1 254 50 303
Bactoprenol glucosyl transferase OS=Salmonella phage P22 OX=10754 GN=gtrB PE=3 SV=1
P77293 4.32e-54 1 257 50 306
Prophage bactoprenol glucosyl transferase homolog OS=Escherichia coli (strain K12) OX=83333 GN=yfdH PE=1 SV=1
O34319 6.90e-54 15 260 68 318
Uncharacterized glycosyltransferase YkcC OS=Bacillus subtilis (strain 168) OX=224308 GN=ykcC PE=3 SV=2
P68667 1.90e-52 1 254 50 303
SfII prophage-derived bactoprenol glucosyl transferase OS=Shigella flexneri OX=623 GN=gtrB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000026 0.000016 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
179 201
208 230