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CAZyme Information: MGYG000001737_00717

You are here: Home > Sequence: MGYG000001737_00717

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 Eubacterium_R sp000434995
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp000434995
CAZyme ID MGYG000001737_00717
CAZy Family GT4
CAZyme Description Glycosyltransferase Gtf1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
372 MGYG000001737_2|CGC2 42188.65 8.9082
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001737 1877486 MAG Sweden Europe
Gene Location Start: 189795;  End: 190913  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001737_00717.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 198 344 6.2e-27 0.9375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 1.61e-56 2 371 1 366
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.
cd03809 GT4_MtfB-like 1.10e-43 2 367 1 361
glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
COG0438 RfaB 7.48e-42 1 372 1 376
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd04955 GT4-like 3.52e-39 2 363 1 371
glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases. 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 in certain bacteria and Archaea.
cd03820 GT4_AmsD-like 2.29e-35 16 365 13 348
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCU04015.1 4.88e-157 5 371 1 367
BBK63254.1 8.63e-155 1 371 7 376
QIB70710.1 5.90e-154 5 372 1 368
QJU17712.1 5.73e-153 5 372 1 367
ANU78560.1 4.67e-152 5 372 1 367

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4X6L_A 5.16e-08 133 370 229 491
ChainA, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_C Chain C, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_D Chain D, TarM [Staphylococcus aureus subsp. aureus 21178],4X7P_A Chain A, TarM [Staphylococcus aureus subsp. aureus 21178],4X7P_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178]
4X7M_A 5.16e-08 133 370 229 491
ChainA, TarM [Staphylococcus aureus subsp. aureus 21178],4X7M_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178],4X7R_A Chain A, TarM [Staphylococcus aureus subsp. aureus 21178],4X7R_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178]
4WAC_A 5.20e-08 133 370 234 496
CrystalStructure of TarM [Staphylococcus aureus],4WAD_A Crystal Structure of TarM with UDP-GlcNAc [Staphylococcus aureus]
6EJJ_A 5.44e-08 16 369 15 353
Structureof a glycosyltransferase / state 2 [Campylobacter jejuni],6EJJ_B Structure of a glycosyltransferase / state 2 [Campylobacter jejuni]
6EJI_A 1.29e-07 16 369 15 353
Structureof a glycosyltransferase [Campylobacter jejuni],6EJI_B Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_A Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_B Structure of a glycosyltransferase [Campylobacter jejuni]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q58577 8.15e-18 16 372 17 348
Uncharacterized glycosyltransferase MJ1178 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1178 PE=3 SV=1
D4GU62 2.69e-11 152 349 166 353
Low-salt glycan biosynthesis hexosyltransferase Agl9 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=agl9 PE=3 SV=1
Q65CC7 9.88e-09 97 333 88 347
Alpha-D-kanosaminyltransferase OS=Streptomyces kanamyceticus OX=1967 GN=kanE PE=1 SV=1
Q0P9C5 6.78e-08 50 369 46 352
GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglH PE=1 SV=1
A0A0H2WWV6 2.83e-07 133 370 229 491
Poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase OS=Staphylococcus aureus (strain COL) OX=93062 GN=tarM 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
1.000035 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001737_00717.