CAZyme Information: MGYG000002210_00288

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; RUG12045
• CAZyme ID: MGYG000002210_00288
• CAZy Family: GT4
• CAZyme Description: D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
734	MGYG000002210_13|CGC1	85088.32	4.7353

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002210	2586109	MAG	Spain	Europe

• Gene Location: Start: 4592; End: 6796 Strand: -

Full Sequence      

MAKWRELTAKTVKTLQKDGPRKVGEKARRYMKRRQAERQEAVYARGDFREVLFINGCDEH
LPHPGRYRVSHQREQLESLGITTGEVYFENLQMETVRCYRVFIFFRCPCTETIRDFVEEA
RRLNKTVLYDVDDLVFDTAYTDQIPYLENMDPEQREAYDENVRSMGRLLDLCDGAITTTA
CLGEALAERVSRVLINRNVASEEMVSLSRQAMAAREEERQEDGRVRLGYFSGSITHNDDF
QMILPALVSLLEQYDHLELYLMGELDLPPQLEPWRDQIELEPFADWRELPARIASVDINL
APLRETVFNRAKSENKWIEAALVKVPTVASDVGAFREMVENGKTGILCRDEQQWKEALQA
LIEQPQYRHIIGEAAFRECAARCVTAASGFSLLQFIRELERPAVIFFLPGFQVSGGVMVA
LQHARLLQESGWDVTLGSIDEEEDRAWYEFEGSRFPVFAAENSRLLTAVDCGVATMWSTC
QCLDKWPSLENRAYLVQNYEPDFYVPGDPLRMQARETYGYHPGWKYLTVSPWCADWLREQ
YGHEAFLVPNGLETAKFYDQQRTMDGKIRILIEGDSTAEHKNVDESFRAAELLEQGKYEI
WYMAYHGEPKDWYRVDKFLPQVPYGQVQEVYRQCDILLKSSLLESFSYPPLEMMASGGFV
VAVENEGNREYLRDGENCLLYPAGEPEAAAEAIRRICRDVQLREHLYAEGQRTAETREWR
QLRQQILEIYRKLI

Enzyme Prediction     

No EC number prediction in MGYG000002210_00288.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	617	705	1e-18	0.55

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	2.99e-25	404	731	2	366	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.
cd03794	GT4_WbuB-like	3.74e-24	120	385	119	382	Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
COG0438	RfaB	7.19e-19	524	734	152	378	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03801	GT4_PimA-like	6.56e-16	162	401	131	363	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.
COG0438	RfaB	1.71e-15	218	401	192	372	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRO35979.1	2.27e-258	1	730	1	722
QBF76212.1	2.27e-258	1	730	1	722
SET96050.1	1.28e-243	43	732	45	730
BBF44263.1	1.51e-229	1	730	1	756
QIA33403.1	1.26e-224	48	730	45	757

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4N9W_A	9.35e-07	527	730	149	364	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	9.76e-07	527	730	165	380	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
Q50864	1.36e-13	461	680	983	1204	O-antigen biosynthesis protein RfbC OS=Myxococcus xanthus OX=34 GN=rfbC PE=4 SV=1
O07147	1.20e-06	617	730	246	360	Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium leprae (strain TN) OX=272631 GN=pimA PE=3 SV=1
P71053	4.99e-06	625	714	263	352	Putative glycosyltransferase EpsD OS=Bacillus subtilis (strain 168) OX=224308 GN=epsD PE=2 SV=1
A0QWG6	5.06e-06	527	730	145	360	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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002210_00288.