CAZyme Information: MGYG000000339_01212

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA9475
• CAZyme ID: MGYG000000339_01212
• CAZy Family: GT4
• CAZyme Description: Putative glycosyltransferase EpsD

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
118	MGYG000000339_181|CGC1	12947.94	6.4384

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000339	1808008	MAG	Sweden	Europe

• Gene Location: Start: 42; End: 398 Strand: +

Full Sequence      

MRFPGQVSDMPTWYAACDVVVSASRIEGLPFNLMEAMYYGRPIVASNVKGHHDLLAPNQA
GLLYPYGDAAACAQQIRDLLAQPQLRQALSTAARQAVTPYLLPTVLPQVMGQYQQLLD

Enzyme Prediction     

No EC number prediction in MGYG000000339_01212.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	2	88	4.7e-20	0.55

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03808	GT4_CapM-like	8.23e-27	2	97	249	344	capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
cd03801	GT4_PimA-like	6.49e-25	2	97	251	348	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
cd03819	GT4_WavL-like	1.11e-24	3	96	242	335	Vibrio cholerae WavL and similar sequences. This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
pfam13692	Glyco_trans_1_4	1.89e-24	2	81	59	137	Glycosyl transferases group 1.
pfam00534	Glycos_transf_1	3.71e-22	2	95	62	157	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALP95402.1	1.79e-25	1	113	252	363
QBB67108.1	1.79e-25	1	113	252	363
QSO47535.1	1.19e-21	1	117	256	372
AQS02350.1	3.34e-21	3	111	260	368
AQS16333.1	3.34e-21	3	111	260	368

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KIH_A	8.71e-10	1	116	306	424	Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus]
4N9W_A	4.21e-07	1	114	249	365	Crystalstructure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_A Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_B Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_C Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_D Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155]
2GEJ_A	4.24e-07	1	114	265	381	CrystalStructure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man [Mycolicibacterium smegmatis MC2 155],2GEK_A Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP [Mycolicibacterium smegmatis MC2 155]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P71053	5.21e-10	3	118	258	373	Putative glycosyltransferase EpsD OS=Bacillus subtilis (strain 168) OX=224308 GN=epsD PE=2 SV=1
O07147	8.53e-09	1	114	245	361	Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium leprae (strain TN) OX=272631 GN=pimA PE=3 SV=1
Q8S4F6	7.93e-08	6	100	366	463	Sulfoquinovosyl transferase SQD2 OS=Arabidopsis thaliana OX=3702 GN=SQD2 PE=1 SV=1
A0QRG8	9.01e-07	14	117	266	367	GDP-mannose-dependent alpha-mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mgtA PE=3 SV=1
A0QWG6	2.30e-06	1	114	245	361	Phosphatidyl-myo-inositol mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=pimA 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000339_01212.