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CAZyme Information: MGYG000000025_01482

You are here: Home > Sequence: MGYG000000025_01482

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 Staphylococcus nepalensis
Lineage Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus nepalensis
CAZyme ID MGYG000000025_01482
CAZy Family GT2
CAZyme Description 4,4'-diaponeurosporenoate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
344 39211.63 9.8639
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000025 2822370 Isolate United Kingdom Europe
Gene Location Start: 206884;  End: 207918  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000025_01482.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 18 115 5.7e-20 0.5941176470588235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04179 DPM_DPG-synthase_like 1.72e-16 19 103 1 91
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.
cd00761 Glyco_tranf_GTA_type 1.75e-16 19 101 1 87
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
cd06439 CESA_like_1 2.07e-16 16 101 30 119
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily. This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.
cd06423 CESA_like 3.48e-16 19 101 1 88
CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.
COG0463 WcaA 1.37e-15 17 298 5 291
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWI43395.1 2.18e-247 1 344 3 346
ATH64032.1 2.18e-247 1 344 3 346
ATH58941.1 2.18e-247 1 344 3 346
ANR67351.1 4.14e-197 1 344 3 346
ANQ65730.1 2.41e-189 1 344 3 346

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3F1Y_A 3.55e-07 11 141 90 232
Mannosyl-3-phosphoglyceratesynthase from Rubrobacter xylanophilus [synthetic construct],3F1Y_C Mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus [synthetic construct],3KIA_A Crystal structure of mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus [synthetic construct],3KIA_C Crystal structure of mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus [synthetic construct],3O3P_A Crystal structure of R. xylanophilus MpgS in complex with GDP-Mannose [Rubrobacter xylanophilus],3O3P_B Crystal structure of R. xylanophilus MpgS in complex with GDP-Mannose [Rubrobacter xylanophilus]
4Y6N_A 2.26e-06 17 102 49 141
Crystalstructure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-1 [Mycobacterium tuberculosis H37Rv],4Y6U_A Mycobacterial protein [Mycobacterium tuberculosis H37Rv],4Y7F_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and 3-(phosphonooxy)propanoic acid (PPA) - GpgS Mn2+ UDP-Glc PPA [Mycobacterium tuberculosis H37Rv],4Y7G_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and glycerol 3-phosphate (G3P) - GpgS Mn2+ UDP-Glc G3P [Mycobacterium tuberculosis H37Rv],4Y9X_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-3 [Mycobacterium tuberculosis H37Rv],5JQX_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_B Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_C Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_D Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JSX_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+ and uridine-diphosphate-glucose (UDP-Glc) [Mycobacterium tuberculosis H37Ra],5JT0_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate (UDP) and glucosyl-3-phosphoglycerate (GPG) - GpgS*GPG*UDP*Mn2+ [Mycobacterium tuberculosis H37Rv],5JUC_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate (UDP) and glucosyl-3-phosphoglycerate (GPG) - GpgS*GPG*UDP*Mn2+_2 [Mycobacterium tuberculosis H37Rv],5JUD_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with uridine-diphosphate (UDP) - GpgS*UDP [Mycobacterium tuberculosis variant bovis AF2122/97]
3E25_A 2.33e-06 17 102 45 137
ChainA, Crystal structure of M. tuberculosis glucosyl-3-phosphoglycerate synthase [Mycobacterium tuberculosis],3E26_A Chain A, Crystal structure of M. tuberculosis glucosyl-3-phosphoglycerate synthase [Mycobacterium tuberculosis]
4DDZ_A 2.37e-06 17 102 65 157
Crystalstructure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis [Mycobacterium tuberculosis H37Rv],4DE7_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mg2+ and uridine-diphosphate (UDP) [Mycobacterium tuberculosis H37Rv],4DEC_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate (UDP) and phosphoglyceric acid (PGA) [Mycobacterium tuberculosis H37Rv],5JQQ_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis - apo form [Mycobacterium tuberculosis H37Ra]
5MLZ_A 4.53e-06 17 107 25 119
Dolichylphosphate mannose synthase in complex with GDP and Mg2+ [Pyrococcus furiosus DSM 3638],5MM0_A Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex) [Pyrococcus furiosus DSM 3638],5MM1_A Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose [Pyrococcus furiosus DSM 3638]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q99R74 1.99e-93 7 344 31 371
4,4'-diaponeurosporenoate glycosyltransferase OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=crtQ PE=3 SV=1
Q7A3E0 1.99e-93 7 344 31 371
4,4'-diaponeurosporenoate glycosyltransferase OS=Staphylococcus aureus (strain N315) OX=158879 GN=crtQ PE=1 SV=1
Q6GDN6 3.98e-93 13 344 37 371
4,4'-diaponeurosporenoate glycosyltransferase OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=crtQ PE=3 SV=1
Q5HCY7 5.63e-93 13 344 37 371
4,4'-diaponeurosporenoate glycosyltransferase OS=Staphylococcus aureus (strain COL) OX=93062 GN=crtQ PE=3 SV=2
Q8NUQ4 5.63e-93 13 344 37 371
4,4'-diaponeurosporenoate glycosyltransferase OS=Staphylococcus aureus (strain MW2) OX=196620 GN=crtQ PE=3 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
1.000089 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
251 270
274 296
301 323