CAZyme Information: MGYG000000822_02122

Basic Information

• Species: Companilactobacillus farciminis_A
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Companilactobacillus; Companilactobacillus farciminis_A
• CAZyme ID: MGYG000000822_02122
• CAZy Family: GT2
• CAZyme Description: putative glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
322		36674.56	9.6866

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000822	2370791	MAG	China	Asia

• Gene Location: Start: 13846; End: 14814 Strand: +

Full Sequence      

MKNQLISIVLPVFNEEAGIQATIDTLLNYIEQQEEKYELIFVDDGSKDKSVAIIKRALAQ
NDHIKLVEFSRNFGHQLAITAGLEYTKGDAVVVMDADLQDPPEVIPQMIKKWHEGYQIVY
GKRMQRDGETVFKKFTAKMFYRTFQKLATINMPLDTGDFRLMDRRAVQQLLKLHEKDPFV
RGQVTWIGFKQTSVLYHRQERIAGETKYPLSKMIKLAVDGITSFSMKPLHFVNLFSVLPL
ASGVFSLGYLIATNSYSFASIGVTVLLFTLGLLMLSIGILGSYLGRVLDQVNNRPRYIVS
KTEGFEERNKGIHHFSARQINN

Enzyme Prediction     

No EC number prediction in MGYG000000822_02122.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	7	170	2e-38	0.9882352941176471

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04187	DPM1_like_bac	1.93e-92	8	189	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	3.99e-66	8	189	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	1.13e-48	6	304	8	313	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
pfam00535	Glycos_transf_2	6.07e-38	7	167	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.
COG0463	WcaA	8.97e-36	5	235	4	231	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMT84428.1	5.87e-229	1	322	1	322
AKS51842.1	5.87e-229	1	322	1	322
AKP03537.1	5.87e-229	1	322	1	322
QCX24338.1	2.56e-223	1	322	1	322
ATO46062.1	5.17e-223	1	322	1	322

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKP_A	1.96e-79	6	306	28	333	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	2.77e-79	6	306	28	333	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	2.94e-14	6	153	25	169	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]
5HEA_A	5.50e-07	4	97	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]
4Y6N_A	8.38e-06	6	119	49	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34319	4.56e-105	7	308	8	314	Uncharacterized glycosyltransferase YkcC OS=Bacillus subtilis (strain 168) OX=224308 GN=ykcC PE=3 SV=2
Q55487	5.33e-79	6	306	5	310	Uncharacterized glycosyltransferase sll0501 OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=sll0501 PE=1 SV=1
P74505	2.87e-76	7	307	24	329	Uncharacterized glycosyltransferase slr1943 OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=slr1943 PE=3 SV=1
P57022	9.93e-63	6	306	3	307	Bactoprenol glucosyl transferase OS=Salmonella phage P22 OX=10754 GN=gtrB PE=3 SV=1
P68667	3.83e-62	6	302	3	304	SfII prophage-derived bactoprenol glucosyl transferase OS=Shigella flexneri OX=623 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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
231	253
263	285