CAZyme Information: MGYG000001080_01143

Basic Information

• Species: Staphylococcus haemolyticus_A
• Lineage: Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus haemolyticus_A
• CAZyme ID: MGYG000001080_01143
• CAZy Family: GT2
• CAZyme Description: Putative glycosyltransferase CsbB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
186		21317.81	8.9495

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001080	1416081	MAG	Sweden	Europe

• Gene Location: Start: 2725; End: 3285 Strand: -

Full Sequence      

MINSFVEDIEFIDGVGDFRLLSQRAVKSIASLKEYNRFSKGLFEWIGYNTKIFTYQNVER
EAGHSKWTFTKLLNYGIDGLISFNNKPLRAMIYLGMTIFSLSIVYILYLLIGIMVNGINN
PGYFTTIAADLLIGGIQLMSIGVVGEYIGRIYYEVKQRPKYIVQASNLKEPSYDLKLVEQ
EKEKVH

Enzyme Prediction     

No EC number prediction in MGYG000001080_01143.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10714	PRK10714	1.51e-15	59	164	202	309	undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
cd04187	DPM1_like_bac	1.13e-09	8	48	141	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	0.009	4	48	141	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOV86597.1	1.20e-122	1	186	144	329
QUX19622.1	8.03e-121	1	186	144	329
QTK12124.1	8.03e-121	1	186	144	329
QTK09941.1	8.03e-121	1	186	144	329
QXN77528.1	8.03e-121	1	186	144	329

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKP_A	1.98e-39	8	163	171	326	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	1.09e-38	8	163	171	326	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45539	1.40e-62	2	175	143	313	Putative glycosyltransferase CsbB OS=Bacillus subtilis (strain 168) OX=224308 GN=csbB PE=2 SV=1
Q55487	6.59e-39	8	163	148	303	Uncharacterized glycosyltransferase sll0501 OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=sll0501 PE=1 SV=1
P57022	1.54e-38	13	169	151	307	Bactoprenol glucosyl transferase OS=Salmonella phage P22 OX=10754 GN=gtrB PE=3 SV=1
P68668	1.64e-37	13	171	151	309	Bactoprenol glucosyl transferase OS=Shigella phage SfII OX=66284 GN=gtrB PE=3 SV=1
P68667	1.64e-37	13	171	151	309	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
1.000042	0.000007	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
90	112
127	149