CAZyme Information: MGYG000000779_01636

Basic Information

• Species: Prevotella sp000431975
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000431975
• CAZyme ID: MGYG000000779_01636
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
382	MGYG000000779_100|CGC1	43214.66	7.2635

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000779	2667664	MAG	Denmark	Europe

• Gene Location: Start: 6523; End: 7671 Strand: -

Full Sequence      

MKLSVIIVNYRVRPYLLQCLRSVFRALDGMDAEVFVVDNHSGDGSVEAVTEHYPQVKLIA
SMHNLGFARANNKAIREAEGDYVLLLNPDTLVGEDVLKRAVAFMDGHPDAGACGVHMLNS
DGSSAPESRRGVPSPLTAFYKMSGLCPHSPKSRRYGRYYMGWLPWNEPVEIDIVSGAFCL
LRREALAEVGLLDETFFMYGEDIDLSYRLLKKGWHNWYLPLRILHYKGESTQKSSFRYVH
VFYEAMLIFFRKHYGHLSWLLSVPVQAGIYLKALQALCLLQFRGARRALGFFTPSMAVST
EAVYVFHGSRSNKEKFDLFCRRRGLMTEPAEGAPVYAVYDVSVYDYTSMLEALASQQCQP
REQLATYDPDADLLITATQVVQ

Enzyme Prediction     

No EC number prediction in MGYG000000779_01636.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	4	189	6.8e-29	0.9882352941176471

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1216	GT2	7.95e-63	1	290	3	284	Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd04186	GT_2_like_c	1.46e-56	5	226	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.
pfam00535	Glycos_transf_2	1.36e-27	4	186	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.
cd02525	Succinoglycan_BP_ExoA	1.32e-20	4	264	3	245	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.
COG1215	BcsA	2.77e-20	2	256	55	304	Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGB27994.1	4.95e-150	1	382	9	400
QYR10757.1	5.76e-146	1	381	1	397
ALO48171.1	2.05e-140	1	382	1	394
ATV51719.1	6.25e-138	1	382	1	398
ATV53967.1	2.52e-137	1	382	1	398

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5TZE_C	5.70e-09	1	128	1	131	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	8.25e-09	1	128	1	131	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]
6P61_A	8.43e-07	4	235	16	211	Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P9WMY2	3.07e-26	3	259	5	267	N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2
P9WMY3	3.07e-26	3	259	5	267	N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2
D4GU63	8.99e-11	3	208	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
P36667	1.72e-08	5	239	4	244	Rhamnosyltransferase WbbL OS=Escherichia coli (strain K12) OX=83333 GN=wbbL PE=1 SV=1
A0A0H3JPC6	4.52e-08	1	128	2	132	Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=tarS PE=1 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
1.000079	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000779_01636.