CAZyme Information: MGYG000000153_01477

Basic Information

• Species: CAG-45 sp000438375
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-45; CAG-45 sp000438375
• CAZyme ID: MGYG000000153_01477
• CAZy Family: GT2
• CAZyme Description: putative glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
314	MGYG000000153_6|CGC1	35872.77	9.2749

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000153	2962513	Isolate	United Kingdom	Europe

• Gene Location: Start: 98040; End: 98984 Strand: -

Full Sequence      

MDNKIKEANFVSAVIYIHNNEREITPFLEWLDTQLDLNFKKYEIICVDDGSMDASEEAVR
AYGKNRAKEAVSLLHMSYFQGLEVAMNAGVDLAIGDFVFEFDTVCMDYKTELLMQVYRRS
LDGFDIVSASAMRKNKWTSNLFYRVFNHFSKTQYKIQNETFRILSRRAINRVHSLSKTIP
YRKVLYANCGLLADCISYTPSQKLERSFSDEQAKMRRTLAVDSLVLFTNIGYKAAVTMTG
VMMVATLAVAIYAVAVFALGNPIQGWTTTILFLAVSFFGLFSILTIIIKYLSLILQLVFK
KQKYSFSSIEKITK

Enzyme Prediction     

No EC number prediction in MGYG000000153_01477.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04187	DPM1_like_bac	3.72e-21	14	187	2	177	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	7.86e-19	20	181	7	175	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.
pfam00535	Glycos_transf_2	9.47e-13	12	171	1	161	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.
cd00761	Glyco_tranf_GTA_type	3.97e-10	13	143	1	130	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
PRK10073	PRK10073	2.42e-09	8	98	5	89	putative glycosyl transferase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW89740.1	6.56e-104	6	314	5	311
BBK78197.1	6.56e-104	6	314	5	311
AHF08061.1	2.18e-95	6	314	5	314
AWW26891.1	9.74e-95	6	313	20	327
AFA49804.1	9.19e-94	6	313	14	321

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EKE_A	1.62e-14	11	190	28	210	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	1.62e-14	11	190	28	210	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]
6P61_A	2.00e-06	6	128	10	127	Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q55487	7.44e-14	11	190	5	187	Uncharacterized glycosyltransferase sll0501 OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=sll0501 PE=1 SV=1
O22007	8.49e-09	11	204	3	199	Bactoprenol glucosyl transferase OS=Shigella phage SfV OX=55884 GN=gtrB PE=3 SV=1
P68667	8.58e-09	11	204	3	199	SfII prophage-derived bactoprenol glucosyl transferase OS=Shigella flexneri OX=623 GN=gtrB PE=3 SV=1
P68668	8.58e-09	11	204	3	199	Bactoprenol glucosyl transferase OS=Shigella phage SfII OX=66284 GN=gtrB PE=3 SV=1
P77293	1.52e-08	11	204	3	199	Prophage bactoprenol glucosyl transferase homolog OS=Escherichia coli (strain K12) OX=83333 GN=yfdH 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
1.000046	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
234	256
271	293