CAZyme Information: MGYG000003576_00682

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; DTU089
• CAZyme ID: MGYG000003576_00682
• CAZy Family: GT2
• CAZyme Description: Prophage bactoprenol glucosyl transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
312		36117.22	8.825

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003576	2097868	MAG	Fiji	Oceania

• Gene Location: Start: 4018; End: 4956 Strand: -

Full Sequence      

MKKIGIVIPCYNEQENIVNICKAVENEIHKSLPKYDYEILVIDNCSTDNTRPLVRELCRQ
NKKIKAIFNAKNFGQFNSPYYAILQSSGDCVIPVCADFQDPVEMIPKFVKEWENGYKIVC
GIKSSSKENRIMRFFRTCYYKLIKKMSSVEQIEHFTGFALYDKSFVQVLRDLKDPTPFIR
GIVAELGFRRKDIEYTQQRRAAGKTHNNFFTLYDAAMLSFTSYTKAGLRIATFVGFSAAI
MSFLVGIIYLILKLVWWDRFPGGAAPTIIILSFLCSLQLFFLGFLGEYIMNMNTRLMNRP
LVVEEERLNFEE

Enzyme Prediction     

No EC number prediction in MGYG000003576_00682.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	6	123	1.2e-23	0.6705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04187	DPM1_like_bac	9.26e-71	6	188	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	2.96e-47	6	188	1	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.
PRK10714	PRK10714	7.82e-26	1	300	5	304	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
COG0463	WcaA	2.50e-21	1	293	2	291	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00535	Glycos_transf_2	1.20e-20	6	146	2	140	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VCV20945.1	1.16e-163	1	312	1	312
QNM10232.1	2.48e-157	2	311	4	313
QWT52122.1	4.06e-157	1	312	1	312
QJU23130.1	1.99e-155	1	312	1	312
QRP37329.1	1.99e-155	1	312	1	312

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKE_A	2.29e-38	3	301	27	323	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	1.71e-37	3	301	27	323	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P57022	2.84e-40	3	300	2	297	Bactoprenol glucosyl transferase OS=Salmonella phage P22 OX=10754 GN=gtrB PE=3 SV=1
P68668	4.14e-39	3	300	2	297	Bactoprenol glucosyl transferase OS=Shigella phage SfII OX=66284 GN=gtrB PE=3 SV=1
P68667	4.14e-39	3	300	2	297	SfII prophage-derived bactoprenol glucosyl transferase OS=Shigella flexneri OX=623 GN=gtrB PE=3 SV=1
Q9T1D6	4.01e-38	3	307	2	304	Bactoprenol glucosyl transferase OS=Shigella phage SfX OX=10874 GN=gtrB PE=3 SV=1
O22007	4.20e-38	3	307	2	305	Bactoprenol glucosyl transferase OS=Shigella phage SfV OX=55884 GN=gtrB PE=3 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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
230	252
267	289