CAZyme Information: MGYG000002382_01248

Basic Information

• Species: Stenotrophomonas maltophilia_AK
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia_AK
• CAZyme ID: MGYG000002382_01248
• CAZy Family: GT2
• CAZyme Description: Dodecaprenyl-phosphate galacturonate synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
240	MGYG000002382_41|CGC2	26828.6	10.5733

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002382	4489830	Isolate	not provided	not provided

• Gene Location: Start: 43480; End: 44202 Strand: +

Full Sequence      

MSQPELSVVVPVFNERDNVAPLVAEITAALRGRLPFEIVYIDDHSRDDTLAVLQGLKATT
PELRVLHHVNQSGQSTAVRTGVKHARAPWIATLDGDGQNDPADIPKLLAARDAAEAQVKL
FAGWRVNRQDSGSKRWASKWANAIRARMLRDDTPDTGCGIKLFERSAFLDLPYFDHMHRY
LPALMQRAGWKTTSVPVNHRHRTAGVSKYNNLGRALVGIRDLRGVAWLITRSKRTAVEER

Enzyme Prediction     

No EC number prediction in MGYG000002382_01248.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	7	168	5.7e-29	0.9705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04179	DPM_DPG-synthase_like	1.14e-52	8	185	1	180	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.
cd04187	DPM1_like_bac	3.96e-51	8	189	1	180	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.
cd06442	DPM1_like	1.93e-34	8	228	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.
COG0463	WcaA	5.46e-28	2	216	1	210	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00535	Glycos_transf_2	1.90e-27	7	168	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
VEF35834.1	3.70e-175	1	240	1	240
ARZ76446.1	3.70e-175	1	240	1	240
SNW15013.1	3.70e-175	1	240	1	240
QNG91211.1	3.70e-175	1	240	1	240
VEE53753.1	3.70e-175	1	240	1	240

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKE_A	6.10e-14	5	210	27	231	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	6.10e-14	5	210	27	231	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	4.46e-13	5	110	24	127	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	6.35e-30	5	229	19	245	Dodecaprenyl-phosphate galacturonate synthase OS=Rhizobium leguminosarum bv. viciae (strain 3841) OX=216596 GN=rgtE PE=1 SV=1
Q48HZ2	1.82e-24	6	210	9	212	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OX=264730 GN=arnC PE=3 SV=1
Q4KC83	1.87e-24	6	210	9	212	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5) OX=220664 GN=arnC PE=3 SV=1
Q8D342	1.06e-23	5	210	6	210	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Wigglesworthia glossinidia brevipalpis OX=36870 GN=arnC PE=3 SV=1
Q2NRV6	4.13e-23	1	210	5	213	Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Sodalis glossinidius (strain morsitans) OX=343509 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
1.000038	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002382_01248.