CAZyme Information: MGYG000001868_01677

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485
• CAZyme ID: MGYG000001868_01677
• CAZy Family: GT2
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
242	MGYG000001868_298|CGC1	27409.66	9.7608

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001868	1969203	MAG	Denmark	Europe

• Gene Location: Start: 902; End: 1630 Strand: +

Full Sequence      

MNPTANYKFTVIVPLYNEEDNIKALEERLGAWLRTAPVESCVLFVDDGSSDSSFTRLKEA
CSRNKDFFYLRLAKNSGLSAALKAGFDATESPWLGYIDADLQTTPEDFPLLLEHAKDYAM
VIGIRADRHDSGFKKLQSKIANGFRRKMTGDGVQDTGCPLKVISTPLAKKLPMFTGLHRF
LPALALLYGEKVKQIPVRHFPRTAGTSKYHLWNRLKGPFLDCFAYRWMRKRLIDNKIAES
NL

Enzyme Prediction     

No EC number prediction in MGYG000001868_01677.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	10	140	2e-24	0.7647058823529411

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04179	DPM_DPG-synthase_like	9.26e-48	11	189	1	184	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.
cd04187	DPM1_like_bac	1.59e-47	11	189	1	180	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.
PRK10714	PRK10714	4.75e-31	8	211	7	212	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
cd04188	DPG_synthase	8.95e-29	11	198	1	203	DPG_synthase is involved in protein N-linked glycosylation. 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.
cd06442	DPM1_like	8.14e-26	11	208	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CUA19725.1	8.48e-123	1	242	1	242
QCT79768.1	1.20e-122	1	242	1	242
AKA52944.1	1.20e-122	1	242	1	242
CBW23766.1	1.20e-122	1	242	1	242
QCQ42854.1	1.20e-122	1	242	1	242

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKE_A	5.95e-16	5	225	24	246	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	8.14e-16	5	213	24	234	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]
5MLZ_A	1.58e-09	8	117	24	130	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8D342	9.60e-31	8	235	6	237	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Wigglesworthia glossinidia brevipalpis OX=36870 GN=arnC PE=3 SV=1
C6DAW6	1.04e-30	10	240	9	244	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pectobacterium carotovorum subsp. carotovorum (strain PC1) OX=561230 GN=arnC PE=3 SV=1
C5BDQ5	1.39e-30	10	211	11	214	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Edwardsiella ictaluri (strain 93-146) OX=634503 GN=arnC PE=3 SV=1
Q6D2F0	2.02e-30	10	240	9	244	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=arnC PE=3 SV=1
Q7N3Q6	7.69e-29	8	209	8	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001868_01677.