CAZyme Information: MGYG000004860_02255

Basic Information

• Species: Levilactobacillus namurensis
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Levilactobacillus; Levilactobacillus namurensis
• CAZyme ID: MGYG000004860_02255
• CAZy Family: GT2
• CAZyme Description: putative glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
314	MGYG000004860_30|CGC2	35483.88	7.0407

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004860	2610545	MAG	China	Asia

• Gene Location: Start: 17012; End: 17956 Strand: +

Full Sequence      

MKKVSLVVPCYNEEESIPLFFQTVSKVIDAMNLPTPTIVPEYIFVDDGSSDNTLAEMKAL
HEAHPETVHYRSFSRNFGKESALAAGLQATTGDYVAVMDVDLQDPPELLPKMVKLIEEDG
YDCVGTIQKDRRGQSRIRAFLSSSFYRVINHLSDVRIEPNARDYRLMTRQFVNTVLDLPE
FNRFSKGIFSWVGYKTTYLTYESQPRAAGTTHWNMRQLFSYSIEGIIDFSNAPLRLATWV
GSISFFLSLIGLIFVVVRALTNGGSSVAGWPSLVVIILLIGGIQLFCLGILGQYISKIYL
ETKHRPKYIVREEK

Enzyme Prediction     

EC	2.4.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	5	133	2e-30	0.7058823529411765

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04187	DPM1_like_bac	2.78e-81	6	194	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	1.03e-59	6	194	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	1.71e-40	1	311	5	309	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
COG0463	WcaA	8.99e-30	1	279	2	272	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00535	Glycos_transf_2	9.45e-30	5	124	1	111	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
QMU07297.1	1.49e-204	1	314	1	313
SMS13897.1	1.74e-203	1	314	1	313
QFR61093.1	1.74e-203	1	314	1	313
AKP65417.1	3.92e-200	1	314	1	313
AYM02848.1	2.27e-199	1	314	1	313

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKP_A	1.08e-76	3	312	27	328	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	6.09e-76	3	312	27	328	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]
5MLZ_A	1.08e-14	3	126	24	138	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]
4Y6N_A	5.97e-06	2	124	47	165	Crystalstructure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-1 [Mycobacterium tuberculosis H37Rv],4Y6U_A Mycobacterial protein [Mycobacterium tuberculosis H37Rv],4Y7F_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and 3-(phosphonooxy)propanoic acid (PPA) - GpgS Mn2+ UDP-Glc PPA [Mycobacterium tuberculosis H37Rv],4Y7G_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and glycerol 3-phosphate (G3P) - GpgS Mn2+ UDP-Glc G3P [Mycobacterium tuberculosis H37Rv],4Y9X_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-3 [Mycobacterium tuberculosis H37Rv],5JQX_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_B Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_C Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_D Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JSX_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+ and uridine-diphosphate-glucose (UDP-Glc) [Mycobacterium tuberculosis H37Ra],5JT0_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate (UDP) and glucosyl-3-phosphoglycerate (GPG) - GpgS*GPG*UDP*Mn2+ [Mycobacterium tuberculosis H37Rv],5JUC_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate (UDP) and glucosyl-3-phosphoglycerate (GPG) - GpgS*GPG*UDP*Mn2+_2 [Mycobacterium tuberculosis H37Rv],5JUD_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with uridine-diphosphate (UDP) - GpgS*UDP [Mycobacterium tuberculosis variant bovis AF2122/97]
3E25_A	6.12e-06	2	124	43	161	ChainA, Crystal structure of M. tuberculosis glucosyl-3-phosphoglycerate synthase [Mycobacterium tuberculosis],3E26_A Chain A, Crystal structure of M. tuberculosis glucosyl-3-phosphoglycerate synthase [Mycobacterium tuberculosis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q55487	2.95e-76	3	312	4	305	Uncharacterized glycosyltransferase sll0501 OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=sll0501 PE=1 SV=1
Q45539	1.65e-75	4	312	6	305	Putative glycosyltransferase CsbB OS=Bacillus subtilis (strain 168) OX=224308 GN=csbB PE=2 SV=1
O22007	1.22e-72	3	314	2	305	Bactoprenol glucosyl transferase OS=Shigella phage SfV OX=55884 GN=gtrB PE=3 SV=1
Q9T1D6	3.26e-72	3	314	2	305	Bactoprenol glucosyl transferase OS=Shigella phage SfX OX=10874 GN=gtrB PE=3 SV=1
P77293	1.34e-71	3	314	2	305	Prophage bactoprenol glucosyl transferase homolog OS=Escherichia coli (strain K12) OX=83333 GN=yfdH PE=1 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
1.000097	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
236	258
273	295