CAZyme Information: MGYG000002701_00181

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Christensenellaceae; QANA01
• CAZyme ID: MGYG000002701_00181
• CAZy Family: GT2
• CAZyme Description: putative glycosyltransferase EpsJ

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
357	MGYG000002701_16|CGC1	40662.34	8.8002

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002701	1575023	MAG	Canada	North America

• Gene Location: Start: 5883; End: 6956 Strand: +

Full Sequence      

MQNPVISFILPVYNGESCLFGAASSVLSEQEIAFELLIVDDGSQDGTAALCDALAQEDAR
VRVFHTQNQGQGKARNLGLRHAQGAYIMFVDADDAVLWQGIRSMLSRAEQGGYDVVCGLY
CRKTQERVELIMGGLPSGEVRKAGTGEQTRLYHCIKTASLFGYLWNKLYRKSFLTAHDLW
LDDIRKVYMEDTLFNLKLWSWQPSYYLLSQPVYVYDASGASTTRRLEPEIAEKNAEMIEQ
LFLYYKRNGCLEENLDVLEPLAMRVFCWSLVKNAPMEGLRFKELKRKIRVFLGNVAISKL
LAQKGAGKGLAQLPSFLQRCFYKLCFYLLKARRAGLLSAMFWLLYPVMKIYILRTVK

Enzyme Prediction     

No EC number prediction in MGYG000002701_00181.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	7	129	6e-29	0.7294117647058823

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00535	Glycos_transf_2	4.16e-31	7	174	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.
cd04179	DPM_DPG-synthase_like	9.84e-26	9	118	2	114	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.
PRK10073	PRK10073	6.23e-24	1	179	1	181	putative glycosyl transferase; Provisional
cd04187	DPM1_like_bac	4.33e-23	8	126	1	121	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.
cd00761	Glyco_tranf_GTA_type	5.26e-22	9	118	2	113	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBE97844.1	1.98e-115	1	357	1	358
QIB54483.1	2.27e-114	1	357	1	358
QMW78998.1	2.27e-114	1	357	1	358
QEK17939.1	5.19e-91	6	357	3	354
BCK85582.1	2.05e-39	2	278	1	269

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HEA_A	3.72e-17	2	96	3	97	CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
3BCV_A	2.48e-13	4	96	5	97	Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
5TZE_C	4.75e-11	7	215	4	202	Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
5TZ8_A	7.19e-11	7	215	4	202	Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]
3L7I_A	3.31e-09	6	107	4	107	Structureof the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_B Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_C Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_D Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P71059	1.12e-28	4	292	3	289	Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
P71057	1.79e-24	1	305	1	302	Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 SV=1
A0A0H2UR96	2.79e-18	2	120	1	120	Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1
Q92IF9	3.50e-17	1	140	290	430	Uncharacterized glycosyltransferase RC0461 OS=Rickettsia conorii (strain ATCC VR-613 / Malish 7) OX=272944 GN=RC0461 PE=3 SV=1
Q57022	7.63e-17	1	131	1	134	Uncharacterized glycosyltransferase HI_0868 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0868 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
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
334	353