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CAZyme Information: MGYG000001268_00576

You are here: Home > Sequence: MGYG000001268_00576

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Rothia mucilaginosa_B
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia mucilaginosa_B
CAZyme ID MGYG000001268_00576
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
347 37688.16 6.758
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001268 1847122 MAG Italy Europe
Gene Location Start: 2311;  End: 3354  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001268_00576.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 166 304 1.6e-20 0.85625

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 1.45e-35 13 347 12 366
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.
cd03823 GT4_ExpE7-like 1.18e-27 14 303 14 324
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).
COG0438 RfaB 1.74e-25 14 347 14 379
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03811 GT4_GT28_WabH-like 1.11e-21 7 303 4 325
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
pfam00534 Glycos_transf_1 2.26e-20 166 310 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BAI65411.1 1.94e-244 3 347 2 346
QXW98969.1 3.30e-200 1 347 1 349
BAS19629.1 2.71e-199 1 347 1 349
ATF62794.1 3.15e-198 1 347 1 349
BAV87415.1 3.86e-154 1 346 1 344

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4N9W_A 1.52e-06 15 300 19 327
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 1.57e-06 15 300 35 343
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      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O07147 2.56e-06 168 310 193 330
Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium leprae (strain TN) OX=272631 GN=pimA PE=3 SV=1
A0QWG6 8.26e-06 15 300 15 323
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 help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000072 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001268_00576.