dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lineage

Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium;

CAZyme ID

MGYG000003805_00471

CAZy Family

GT81

CAZyme Description

Glucosyl-3-phosphoglycerate synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
256		27009.75	6.3403

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003805	2110817	MAG	Canada	North America

Gene Location

Start: 10538; End: 11308 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000003805_00471.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT81	4	232	9.5e-80	0.8088737201365188

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK13915	PRK13915	1.99e-106	3	252	29	300	putative glucosyl-3-phosphoglycerate synthase; Provisional
cd00761	Glyco_tranf_GTA_type	1.24e-18	9	118	1	111	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.
cd04179	DPM_DPG-synthase_like	2.16e-18	9	94	1	89	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.
COG0463	WcaA	4.67e-17	6	94	4	93	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00535	Glycos_transf_2	2.39e-16	8	171	1	164	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQU85171.1	9.36e-111	5	253	1	237
AQQ14957.1	4.17e-110	7	253	16	260
AKV59857.1	1.54e-109	5	253	1	237
QDR78471.1	6.28e-108	5	254	1	242
AIL96687.1	5.53e-107	5	254	1	236

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4Y6N_A	3.81e-57	3	237	45	291	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) - GpgSPGA [Mycobacterium tuberculosis H37Ra],5JQX_B Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgSPGA [Mycobacterium tuberculosis H37Ra],5JQX_C Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgSPGA [Mycobacterium tuberculosis H37Ra],5JQX_D Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgSPGA [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) - GpgSGPGUDPMn2+ [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) - GpgSGPGUDPMn2+_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	4.85e-57	3	237	41	287	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	5.83e-57	3	237	61	307	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]
3CKJ_A	7.80e-57	3	237	46	292	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]
3F1Y_A	1.79e-43	5	230	94	330	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
P9WMW9	1.87e-56	3	237	41	287	Glucosyl-3-phosphoglycerate synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=gpgS PE=1 SV=1
Q7U0E1	1.87e-56	3	237	41	287	Glucosyl-3-phosphoglycerate synthase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=gpgS PE=1 SV=1
P9WMW8	1.87e-56	3	237	41	287	Glucosyl-3-phosphoglycerate synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=gpgS PE=3 SV=1
Q73WU1	4.27e-56	3	237	46	292	Glucosyl-3-phosphoglycerate synthase OS=Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) OX=262316 GN=MAP_2569c PE=1 SV=1
A0R2E6	3.71e-54	3	255	26	299	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
1.000022	0.000013	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000003805_00471.

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