CAZyme Information: MGYG000000353_00237

Basic Information

• Species: UBA7173 sp900548705
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900548705
• CAZyme ID: MGYG000000353_00237
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
268		31244.87	9.4659

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000353	2738445	MAG	Sweden	Europe

• Gene Location: Start: 302858; End: 303664 Strand: -

Full Sequence      

MITMNKLKISLVTVTWNSARTIEDTLRSVLGQTYGNIEHIVVDGGSSDATMDIIRKYAGQ
YNSRRFELKWISEPDNGIYDAMNKGISLASGDVVGMLNSDDFFTYPTVLERVADEFKAIS
QRQELDAVYGDIHYVNPERLDKCVRYYSSKAFSRTKMRMGFMPAHPSFYCRKELYDKLGM
YDISFRIASDFELLLRFIYIHRIRTKYLPLDFVTMRTGGTSTSGFSVHRKIYSEHMRAYK
KNRIYSNFFMEATRYLYKIIEICRSNLS

Enzyme Prediction     

No EC number prediction in MGYG000000353_00237.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	10	145	4.6e-22	0.7529411764705882

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06433	GT_2_WfgS_like	1.91e-83	10	223	1	201	WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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.
cd00761	Glyco_tranf_GTA_type	1.98e-25	12	147	2	131	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.
PRK10063	PRK10063	2.01e-22	9	223	3	203	colanic acid biosynthesis glycosyltransferase WcaE.
pfam00535	Glycos_transf_2	6.12e-22	10	170	1	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.
cd02525	Succinoglycan_BP_ExoA	2.48e-20	8	198	1	191	ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT63359.1	8.20e-114	7	268	1	255
QUT47354.1	6.70e-113	7	268	1	255
AII64087.1	1.86e-111	7	262	1	249
QUT30578.1	6.34e-111	7	268	1	255
BCI64586.1	5.24e-108	7	262	1	249

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3BCV_A	1.07e-07	8	102	6	96	Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
5HEA_A	1.58e-06	9	102	7	96	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
P9WMX8	3.84e-23	9	196	7	183	Uncharacterized glycosyltransferase MT1564 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1564 PE=3 SV=1
P9WMX9	3.84e-23	9	196	7	183	Uncharacterized glycosyltransferase Rv1514c OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv1514c PE=1 SV=1
P0A5A0	1.29e-19	10	208	7	192	PGL/p-HBAD biosynthesis glycosyltransferase Mb2981 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB2981 PE=3 SV=1
P9WMX6	1.29e-19	10	208	7	192	PGL/p-HBAD biosynthesis glycosyltransferase MT3031 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3031 PE=3 SV=1
A5U6W5	1.29e-19	10	208	7	192	PGL/p-HBAD biosynthesis glycosyltransferase MRA_2984 OS=Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) OX=419947 GN=MRA_2984 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
1.000086	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000353_00237.