CAZyme Information: MGYG000001017_00638

Basic Information

• Species: Lactococcus garvieae_B
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Lactococcus; Lactococcus garvieae_B
• CAZyme ID: MGYG000001017_00638
• CAZy Family: GT2
• CAZyme Description: Poly-beta-1,6-N-acetyl-D-glucosamine synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
238	MGYG000001017_29|CGC1	27081.16	4.6669

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001017	1758548	MAG	Bangladesh	Asia

• Gene Location: Start: 532; End: 1248 Strand: +

Full Sequence      

MISDIFSQMFTSDSGLQTVITVCLIILCLYPVIGALFWFFGSLSYRFLKKGRKETNFVEL
APDEQPMITIMIPAHNEEVMIEETIEYLATMLNYSNYEILVINDGSTDQTLPILQRLQEK
YEKLRVINILKNQGKAHGFNIGTYFAKGEYILSNDADSIPERDALMKYMNYFMSEIDVNT
AAVTANMDVQNRTTIMGKSQTVEFSSIVGVIKRSQTAINDSMYSYSGANTMYKKTIFD

Enzyme Prediction     

No EC number prediction in MGYG000001017_00638.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	69	236	1.9e-28	0.9647058823529412

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK11204	PRK11204	2.75e-62	24	235	11	219	N-glycosyltransferase; Provisional
cd06423	CESA_like	4.61e-48	70	238	1	167	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.
PRK14583	hmsR	9.38e-34	22	234	29	239	poly-beta-1,6 N-acetyl-D-glucosamine synthase.
COG1215	BcsA	2.15e-31	27	238	15	227	Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
cd00761	Glyco_tranf_GTA_type	6.47e-26	70	186	1	114	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAV01651.1	6.00e-159	1	234	1	234
QSR11691.1	1.40e-157	1	234	1	234
QSR13370.1	1.40e-157	1	234	1	234
QSR03529.1	1.40e-157	1	234	1	234
QSQ99122.1	1.62e-156	1	234	1	234

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YV7_B	1.93e-09	59	165	33	145	MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6YV7_A	1.93e-09	59	165	34	146	MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
5EKE_A	1.51e-08	68	157	28	119	Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa]
5EKP_A	1.51e-08	68	157	28	119	Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa]
5HEA_A	2.37e-08	63	161	2	98	CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q7A351	3.59e-31	27	235	7	211	Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain N315) OX=158879 GN=icaA PE=3 SV=1
Q5HCN1	3.59e-31	27	235	7	211	Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain COL) OX=93062 GN=icaA PE=3 SV=1
Q6GDD8	3.59e-31	27	235	7	211	Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=icaA PE=3 SV=1
Q99QX3	3.59e-31	27	235	7	211	Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=icaA PE=3 SV=1
Q9RQP9	3.59e-31	27	235	7	211	Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=icaA PE=3 SV=2

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
1.000092	0.000005	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
20	42