CAZyme Information: MGYG000001408_01100

Basic Information

• Species: Brevibacterium senegalense
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Brevibacteriaceae; Brevibacterium; Brevibacterium senegalense
• CAZyme ID: MGYG000001408_01100
• CAZy Family: GT81
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
273	MGYG000001408_2|CGC4	29151	8.5532

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001408	3398887	Isolate	not provided	not provided

• Gene Location: Start: 537246; End: 538067 Strand: -

Full Sequence      

MSEEQTPSSVAVIIPAKDEAERIAATVASALTIPGADLVLVVDDGSTDDTGRRAREAGAQ
VVTHSTNRGKAQAMMTGSFAVRNREISQLEPGARHRHRALLFIDGDLEDTAAATAPLAQP
ILAGEADATIAILPAQKRKGGGFGLVVGLAKSGIERLSGFRATQPLSGMRCMTREAFDAT
QPFAAGWGVETGMTIDLVWAGMRVREVECDLQHRVTGRDFKAQLHRAAQYRDVARALAAR
ELRARLTGGRRRTVEQPPVPRPDGPRDAQDGTA

Enzyme Prediction     

No EC number prediction in MGYG000001408_01100.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT81	5	226	5.2e-19	0.7679180887372014

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04179	DPM_DPG-synthase_like	1.88e-23	12	179	1	165	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.
PRK13915	PRK13915	6.81e-17	3	197	26	225	putative glucosyl-3-phosphoglycerate synthase; Provisional
pfam00535	Glycos_transf_2	1.78e-16	12	171	2	153	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.
COG0463	WcaA	3.92e-14	10	252	5	237	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd06423	CESA_like	4.80e-14	12	107	1	109	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPS34217.1	1.58e-124	1	245	1	245
QQT70218.1	1.58e-124	1	245	1	245
QPR42776.1	1.58e-124	1	245	1	245
QPR38610.1	1.58e-124	1	245	1	245
QQB14823.1	6.78e-122	1	245	1	245

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3CKJ_A	4.23e-07	9	196	49	243	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	3.27e-06	9	196	48	242	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	3.34e-06	9	196	44	238	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	3.39e-06	9	196	64	258	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D4GYG3	2.69e-07	6	219	3	203	Glycosyltransferase AglJ OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=aglJ PE=1 SV=1
Q73WU1	2.31e-06	9	196	49	243	Glucosyl-3-phosphoglycerate synthase OS=Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) OX=262316 GN=MAP_2569c PE=1 SV=1
P33700	2.40e-06	7	73	6	77	Succinoglycan biosynthesis protein ExoU OS=Rhizobium meliloti (strain 1021) OX=266834 GN=exoU PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000071	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001408_01100.