CAZyme Information: MGYG000003742_00853

Basic Information

• Species: Prevotella buccalis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella buccalis
• CAZyme ID: MGYG000003742_00853
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
399	MGYG000003742_18|CGC2	45599.71	8.2076

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003742	2540681	MAG	Canada	North America

• Gene Location: Start: 36016; End: 37215 Strand: +

Full Sequence      

MQGVKLSVIIVNYNVKYYLEQCLISLTRSLKDVDAEIFVVDNASVDGSVDYLSVRFPTVN
LISSNHNLGFARANNLAIRQSKGEYVLLLNPDTIVGEHTMRQLIDWMDSHEGVGGVGVRM
MNQQGFDAKESRRGVPTPWTAFYKMCGLCAKHPTSKRFAKYYMGHLPWDEPAEIEIVSGA
FFAVPRKALEDVGLLDEDFFMYGEDIDLSYRLLQKGYHNWYLPLRILHYKGESTQKSSYR
YVHVFYQAMLIFFKKHYGGMSILLGLPIKMAIYAKAFMALVSMQMVKAKQGVGLFRAKKH
ETVRYLFIGSSQSMRECEEIVRRKGLCAQFVTSTYRDHPDGHLTLKLPQADKVYVVYDTQ
TYNFDEVLNIFASQPSEKVCLGTYLPETKMVVTESEIFS

Enzyme Prediction     

No EC number prediction in MGYG000003742_00853.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	7	192	9.3e-21	0.9882352941176471

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04186	GT_2_like_c	1.28e-55	8	229	1	165	Subfamily of Glycosyltransferase Family GT2 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.
COG1216	GT2	1.33e-53	5	299	4	294	Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd00761	Glyco_tranf_GTA_type	3.33e-18	8	128	1	126	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.
pfam00535	Glycos_transf_2	8.81e-18	7	127	1	123	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	1.02e-16	7	241	3	223	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
QYR10757.1	3.13e-162	5	397	2	396
EFC71732.1	2.32e-159	5	398	3	396
QUB47017.1	3.56e-156	5	397	4	395
ATV51719.1	3.25e-152	5	397	2	396
AGB27994.1	2.00e-151	5	397	10	398

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5TZE_C	1.42e-06	5	118	2	128	Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
5TZ8_A	1.91e-06	5	118	2	128	Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WMY2	3.44e-16	6	259	5	266	N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2
P9WMY3	3.44e-16	6	259	5	266	N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2
D4GU63	3.82e-12	6	211	20	205	Low-salt glycan biosynthesis hexosyltransferase Agl10 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=agl10 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
1.000026	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
259	281