CAZyme Information: MGYG000001269_00468

Basic Information

• Species: Rothia mucilaginosa
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia mucilaginosa
• CAZyme ID: MGYG000001269_00468
• CAZy Family: GT4
• CAZyme Description: D-inositol-3-phosphate glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
214	MGYG000001269_10|CGC1	23162.2	4.3017

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001269	2178797	MAG	Italy	Europe

• Gene Location: Start: 27; End: 671 Strand: +

Full Sequence      

MARACPGSELFANWVSGVSTELDHRVGERRLRVGYLGRLTPSKGIATLCQAMSSLNANGI
EYDLVIGGEPVFASDEERAEVEDALARVAAFSTRMGWTTPDRLFGDIDMLVVPSIAPESF
GLVVAEAMSARVPVIVSDAGALSEVLGGASYPYVVPADQPVALAQAIKSLGTELREDTDA
LAERTSELFWRWQENYSPEAGQVRVGEILERFIR

Enzyme Prediction     

No EC number prediction in MGYG000001269_00468.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	33	170	5.8e-21	0.85

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03823	GT4_ExpE7-like	5.57e-28	25	170	186	324	glycosyltransferase ExpE7 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
cd03801	GT4_PimA-like	2.25e-27	23	214	185	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.
COG0438	RfaB	7.96e-26	28	214	197	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00534	Glycos_transf_1	7.23e-23	33	177	5	150	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.
pfam13692	Glyco_trans_1_4	7.71e-20	30	170	1	135	Glycosyl transferases group 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAI65411.1	1.45e-144	1	214	133	346
QXW98969.1	8.37e-109	1	214	134	349
BAS19629.1	1.94e-107	1	214	134	349
ATF62794.1	8.50e-104	1	214	134	349
BAV87415.1	1.95e-68	1	213	134	344

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4N9W_A	5.58e-07	35	167	197	327	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	5.68e-07	35	167	213	343	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
O07147	1.65e-06	35	177	193	330	Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium leprae (strain TN) OX=272631 GN=pimA PE=3 SV=1
A0QWG6	3.04e-06	35	167	193	323	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
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001269_00468.