CAZyme Information: MGYG000003287_02578

Basic Information

• Species: Prevotella melaninogenica
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella melaninogenica
• CAZyme ID: MGYG000003287_02578
• CAZy Family: GT2
• CAZyme Description: Dodecaprenyl-phosphate galacturonate synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
317		36694.41	7.071

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003287	3259243	MAG	United States	North America

• Gene Location: Start: 41169; End: 42122 Strand: -

Full Sequence      

MDISVIIPLYNEEESLPELHAWIQRVMNANGFTYEIIFINDGSKDRSWDVIEDLHHKDEE
HVHAIKFRRNYGKSPALYCGFNAAQGDVVITMDADLQDSPDEIPELYRMIMEEKYDLVSG
YKQKRYDPLTKTIPTKLFNATARKISGVHNLHDFNCGLKAYRRDVVKNIEVYGEMHRYIP
YLAKEAGFVRIGEKVVQHQARKYGKSKFGINRFFNGYLDLLTLWFLTNFGKKPMHVFGLM
GSFMFFIGFIAFLWLIVEKVIMLVNGVYGDLLSDHASFFIALVAMVLGTQLFLAGFIGDL
ISRSNPRRNDYQIEKEM

Enzyme Prediction     

No EC number prediction in MGYG000003287_02578.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	4	168	2.8e-33	0.9823529411764705

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04187	DPM1_like_bac	1.00e-81	5	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	4.37e-62	5	180	1	177	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	2.13e-51	3	303	8	295	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
cd06442	DPM1_like	3.15e-35	5	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.
pfam00535	Glycos_transf_2	2.19e-32	4	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASE17216.1	1.11e-235	1	317	1	317
ADK95563.1	4.76e-235	1	317	40	356
QUB55519.1	3.71e-234	1	317	1	317
QUB62250.1	3.71e-234	1	317	1	317
QUB58125.1	3.71e-234	1	317	1	317

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKE_A	8.29e-28	1	303	26	313	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	2.20e-27	1	303	26	313	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	1.01e-19	1	207	23	230	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
Q1MJ95	4.25e-50	1	307	18	319	Dodecaprenyl-phosphate galacturonate synthase OS=Rhizobium leguminosarum bv. viciae (strain 3841) OX=216596 GN=rgtE PE=1 SV=1
Q02R24	2.82e-47	3	303	9	296	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pseudomonas aeruginosa (strain UCBPP-PA14) OX=208963 GN=arnC PE=3 SV=1
A6V1P1	2.82e-47	3	303	9	296	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pseudomonas aeruginosa (strain PA7) OX=381754 GN=arnC PE=3 SV=1
Q9HY64	2.82e-47	3	303	9	296	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=arnC PE=3 SV=1
B7VBN3	2.82e-47	3	303	9	296	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pseudomonas aeruginosa (strain LESB58) OX=557722 GN=arnC 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
1.000056	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
208	227
234	256
276	298