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CAZyme Information: MGYG000001148_01672

You are here: Home > Sequence: MGYG000001148_01672

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 Fusobacterium_A varium_A
Lineage Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Fusobacterium_A; Fusobacterium_A varium_A
CAZyme ID MGYG000001148_01672
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
236 MGYG000001148_183|CGC1 27141.12 9.0726
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001148 3218254 MAG China Asia
Gene Location Start: 4342;  End: 5052  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001148_01672.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 5 163 1.9e-33 0.9705882352941176

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04187 DPM1_like_bac 1.99e-66 6 185 1 181
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.
cd04179 DPM_DPG-synthase_like 4.64e-56 6 179 1 179
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.
PRK10714 PRK10714 1.18e-45 1 210 5 215
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
pfam00535 Glycos_transf_2 2.16e-34 5 163 1 164
Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd06442 DPM1_like 1.18e-33 6 203 1 208
DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBA50720.1 2.14e-172 1 236 1 236
VEH39580.1 1.45e-170 1 236 1 236
AVQ31613.1 1.45e-170 1 236 1 236
SQJ00561.1 2.58e-164 1 236 1 236
AVQ28669.1 2.58e-164 1 236 1 236

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5MLZ_A 1.24e-18 3 203 24 230
Dolichylphosphate mannose synthase in complex with GDP and Mg2+ [Pyrococcus furiosus DSM 3638],5MM0_A Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex) [Pyrococcus furiosus DSM 3638],5MM1_A Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose [Pyrococcus furiosus DSM 3638]
5EKE_A 2.81e-16 4 231 28 257
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]
5EKP_A 5.27e-16 4 204 28 230
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]
5HEA_A 6.07e-12 2 95 5 94
CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
6P61_A 8.06e-09 4 116 15 126
Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8D342 1.15e-44 2 228 5 235
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Wigglesworthia glossinidia brevipalpis OX=36870 GN=arnC PE=3 SV=1
Q8XDZ5 2.66e-42 1 216 7 223
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Escherichia coli O157:H7 OX=83334 GN=arnC PE=3 SV=1
B5YX45 2.66e-42 1 216 7 223
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Escherichia coli O157:H7 (strain EC4115 / EHEC) OX=444450 GN=arnC PE=3 SV=1
Q32DT4 7.39e-42 1 216 7 223
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Shigella dysenteriae serotype 1 (strain Sd197) OX=300267 GN=arnC PE=3 SV=2
Q7N3Q6 7.93e-42 1 204 6 211
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) OX=243265 GN=arnC PE=2 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
1.000054 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001148_01672.