CAZyme Information: MGYG000001712_00486

Basic Information

• Species: Bacillus_A thuringiensis_S
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A thuringiensis_S
• CAZyme ID: MGYG000001712_00486
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
518		57328.15	7.5192

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001712	5736823	Isolate	United States	North America

• Gene Location: Start: 476587; End: 478143 Strand: +

Full Sequence      

MKKTMAKSLSVIIPASNEVDTISDVIQSVKPLNPVEIIVIANGCNDGTEEVANRLGCKVI
RHTELLGNDVGRAVGAKYAIGDVLLFIDGDFAIPTSKLQLFLNPILHDQTDIVLNNLDAL
FLKKQKPHSVTVWRQILNAMLEREELKIDSLLSVPHALTKEVVQSIGYECLVNPIVAHLR
IAQSKWRISRHCAIDVITPNKFRPVEHAAYGTSLSQSERRMIGDHIEAVAERIVSSDTRG
GYYDGNRKRNSVYHTLNFEDFYQGWGVTSNLYKGKQLSVVIPVQDEEKTIGNVIEELRKI
EPFEIIVVVNGSSDKTATIAKDKGATTIVYKEALGNDVGRSLGTYFAKGEIVLFIDGDFV
IPARELYPFAKAIADGKDVALNDLNHYLDLRVPLHLVTAFKYALNLACDRKDLGVGSLIA
VPNAFSHKCLKAIGYKSLLSPCVAQVKALLSGFEIACVYRVEVDKMNRIRPSEHFAKIGH
PPAVLRIIGDHIEGLEQIIALTDNRGGFYDGNRKRDVL

Enzyme Prediction     

No EC number prediction in MGYG000001712_00486.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	10	124	1.1e-17	0.7176470588235294
GT2	278	390	1.6e-16	0.711764705882353

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04179	DPM_DPG-synthase_like	2.26e-17	11	114	1	113	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.
cd04179	DPM_DPG-synthase_like	4.42e-16	279	381	1	113	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.
COG0463	WcaA	6.80e-15	275	376	3	110	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00535	Glycos_transf_2	8.94e-15	10	114	1	112	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.
PRK13915	PRK13915	8.26e-14	273	358	29	125	putative glucosyl-3-phosphoglycerate synthase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQY36964.1	0.0	1	518	1	518
AFQ17156.1	0.0	5	518	1	514
QGV10141.1	0.0	5	518	1	514
AJQ62226.1	0.0	5	518	1	514
QWS48150.1	0.0	5	518	1	514

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q58619	1.05e-06	276	381	18	127	Uncharacterized protein MJ1222 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1222 PE=4 SV=1
Q2YWE6	6.93e-06	226	358	4	128	4,4'-diaponeurosporenoate glycosyltransferase OS=Staphylococcus aureus (strain bovine RF122 / ET3-1) OX=273036 GN=crtQ PE=3 SV=1
Q6GDN6	9.19e-06	226	358	4	128	4,4'-diaponeurosporenoate glycosyltransferase OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=crtQ 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
1.000084	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001712_00486.