CAZyme Information: MGYG000000187_01809

Basic Information

• Species: Lachnospira sp003537285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp003537285
• CAZyme ID: MGYG000000187_01809
• CAZy Family: GT2
• CAZyme Description: Polyprenol monophosphomannose synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
248		28264.88	9.1402

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000187	2804290	Isolate	China	Asia

• Gene Location: Start: 10555; End: 11301 Strand: +

Full Sequence      

MLSVVIPTFNESKNIRNLVAQIDVALKGVDYEIVFVDDSKDNTPDVIMEVAKEYPQVRME
HRKNGTGLATAVLDGFKLAKGEYMACMDADLQHPPIVLKYMYKAMESGADFCIPSRLIPG
GDDGGLNWYRKFVSGTARKIGQVMLPCLRKISDPTSGLFMFRREVIENADLQPIGWKIMV
EVLAMGTYSKVVEIPYKFQQRTEGESKLSGKVTLEYLKQLKNLRKRYNKSNRYEVEIWST
ERMMKGDK

Enzyme Prediction     

EC	2.4.1.83

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	3	167	1.7e-32	0.9764705882352941

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06442	DPM1_like	3.16e-90	4	223	1	224	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.
cd04179	DPM_DPG-synthase_like	1.56e-51	4	184	1	183	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.
PLN02726	PLN02726	1.98e-36	3	223	12	239	dolichyl-phosphate beta-D-mannosyltransferase
pfam00535	Glycos_transf_2	5.64e-36	3	166	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.
cd04187	DPM1_like_bac	2.89e-33	4	168	1	161	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR71186.1	3.55e-177	1	248	1	248
QAT51234.1	7.76e-84	2	243	1	243
ABI69448.1	1.87e-79	2	223	6	226
AWI06118.1	2.56e-79	1	233	1	233
AKA67428.1	1.03e-78	1	233	1	233

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5MLZ_A	1.60e-61	3	225	26	248	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	1.59e-09	2	207	28	229	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	1.59e-09	2	207	28	229	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]
3BCV_A	7.65e-09	3	90	8	94	Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14020	2.04e-38	3	223	6	234	Dolichol-phosphate mannosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=DPM1 PE=1 SV=3
P54856	4.81e-30	3	223	31	259	Dolichol-phosphate mannosyltransferase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=DPM1 PE=3 SV=2
Q9LM93	5.60e-27	3	220	16	239	Dolichol-phosphate mannosyltransferase subunit 1 OS=Arabidopsis thaliana OX=3702 GN=DPMS1 PE=1 SV=1
A0QZ12	4.96e-23	4	210	26	238	Polyprenol monophosphomannose synthase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=ppm1 PE=1 SV=1
O60762	3.31e-22	3	223	28	256	Dolichol-phosphate mannosyltransferase subunit 1 OS=Homo sapiens OX=9606 GN=DPM1 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
1.000031	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000187_01809.