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CAZyme Information: MGYG000001544_01237

You are here: Home > Sequence: MGYG000001544_01237

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 Corynebacterium bouchesdurhonense
Lineage Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium bouchesdurhonense
CAZyme ID MGYG000001544_01237
CAZy Family GT81
CAZyme Description Glucosyl-3-phosphoglycerate synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
251 26403.05 5.1668
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001544 2255536 Isolate not provided not provided
Gene Location Start: 294409;  End: 295164  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001544_01237.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT81 8 239 3.3e-80 0.8191126279863481

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK13915 PRK13915 9.29e-81 10 243 33 276
putative glucosyl-3-phosphoglycerate synthase; Provisional
cd04179 DPM_DPG-synthase_like 1.17e-08 12 92 1 84
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.
cd02522 GT_2_like_a 1.35e-08 10 89 1 74
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function. Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
COG0463 WcaA 1.51e-08 10 89 5 85
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd00761 Glyco_tranf_GTA_type 2.05e-08 12 92 1 82
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQQ14957.1 1.05e-118 1 250 7 262
QNP91037.1 6.32e-114 10 248 3 234
AIL96687.1 2.17e-112 10 249 3 236
QNP94826.1 3.58e-111 10 249 3 236
AIJ33263.1 1.52e-108 10 249 6 247

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3CKJ_A 1.18e-63 10 235 50 287
CrystalStructure of a Mycobacterial Protein [Mycobacterium avium subsp. paratuberculosis],3CKN_A Crystal Structure of a Mycobacterial Protein [Mycobacterium avium subsp. paratuberculosis],3CKO_A Crystal Structure of a Mycobacterial Protein [Mycobacterium avium subsp. paratuberculosis],3CKQ_A Crystal Structure of a Mycobacterial Protein [Mycobacterium avium subsp. paratuberculosis],3CKV_A Crystal Structure of a Mycobacterial Protein [Mycobacterium avium subsp. paratuberculosis]
4Y6N_A 1.15e-60 10 235 49 286
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 1.48e-60 10 235 45 282
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 1.78e-60 10 235 65 302
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]
3F1Y_A 6.79e-46 10 246 96 343
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q73WU1 6.47e-63 10 235 50 287
Glucosyl-3-phosphoglycerate synthase OS=Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) OX=262316 GN=MAP_2569c PE=1 SV=1
P9WMW8 5.65e-60 10 235 45 282
Glucosyl-3-phosphoglycerate synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=gpgS PE=3 SV=1
P9WMW9 5.65e-60 10 235 45 282
Glucosyl-3-phosphoglycerate synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=gpgS PE=1 SV=1
Q7U0E1 5.65e-60 10 235 45 282
Glucosyl-3-phosphoglycerate synthase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=gpgS PE=1 SV=1
A0R2E6 7.91e-58 10 235 30 264
Glucosyl-3-phosphoglycerate synthase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=gpgS 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
1.000081 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001544_01237.