CAZyme Information: MGYG000001640_01611

Basic Information

• Species: Duncaniella sp900549445
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Duncaniella; Duncaniella sp900549445
• CAZyme ID: MGYG000001640_01611
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
340		38530.86	6.6433

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001640	2860567	MAG	United States	North America

• Gene Location: Start: 3165; End: 4187 Strand: -

Full Sequence      

MENQPQNKPVAVIILNWNGEKFLREYLPSVVKHTPEDIADVIVADNGSTDGSMELLREDF
PTVKVVALDRNYGFAEGYNRAIAMTRYRYTVLLNSDVEVKSDWLTPLYRFMESHPQAGAV
QPKILSLTDPEKFEYAGAAGGFLDCNGFPYCRGRIFDTIETDNGQYDEPMRIFWASGACL
MVDTALYESTGGLDASFFAHMEEIDLCWRMQLAGREVWAVPQAAVYHLGGGSLPASNPRK
TYLNFRNNLLMLRKNLPPQGRTWKLIRRRMIDTIAWAKFALTLRWGNAAAVFRAHRDASR
MFAQYDNGSPEPDRDLIAGNPDIITSYYLRGKKLFSSLNQ

Enzyme Prediction     

No EC number prediction in MGYG000001640_01611.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	12	124	2.9e-22	0.6764705882352942

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04186	GT_2_like_c	6.35e-56	12	229	1	166	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	3.07e-53	10	293	5	277	Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd00761	Glyco_tranf_GTA_type	1.08e-22	12	137	1	128	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	4.00e-20	12	121	2	113	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.
cd04185	GT_2_like_b	3.71e-13	12	251	1	202	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCP73803.1	1.53e-173	10	336	12	337
QCD40751.1	1.53e-173	10	336	12	337
QCD43479.1	1.47e-162	11	340	12	341
QCD36115.1	4.14e-155	8	339	3	331
QQR09216.1	3.29e-143	11	338	10	334

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P61_A	1.44e-08	10	133	15	139	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	4.87e-16	10	227	5	235	N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2
P9WMY3	4.87e-16	10	227	5	235	N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2
D4GU63	1.65e-10	10	250	20	247	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
Q50864	2.36e-07	10	227	576	792	O-antigen biosynthesis protein RfbC OS=Myxococcus xanthus OX=34 GN=rfbC PE=4 SV=1
Q8IA43	8.06e-07	6	229	164	393	Putative polypeptide N-acetylgalactosaminyltransferase 10 OS=Drosophila melanogaster OX=7227 GN=pgant10 PE=2 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
1.000075	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001640_01611.