CAZyme Information: MGYG000001921_01820

Basic Information

• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia
• CAZyme ID: MGYG000001921_01820
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
343		39964.01	8.8146

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001921	2759672	MAG	Denmark	Europe

• Gene Location: Start: 56692; End: 57723 Strand: +

Full Sequence      

MISAILLCYNQKRFIKEQFRAILRQDYPGEWEIIISDDFSQDGSFECLEEMVEKEGEGRR
IILHRNESNRGIAGNLQRAVHLSRGEWIIKFDGDDIAREDRISSLVSLAEKYPGHLVYCH
SYNEINEDGQPAYGRMLPDSDSVVVKPYRECIFDISHVYSCFGGNAMYHRSLFSDFEYLP
SGPGIADDTMLSMRAYLKKSGMVASGKRCSYYRRHNSNICNFKSGNPRTILIKRSEFLIT
TWIMIMKEVYGKHKSGEITYQTADRLMRLIQAEQRRLLLFPYASFDNSLLTKLKWFWNIL
QCRPGLWLVSIPRLLPFCLLQRYLNIKDRIKSLPFFTNHRGSA

Enzyme Prediction     

No EC number prediction in MGYG000001921_01820.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	3	174	1.9e-25	0.9764705882352941

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04196	GT_2_like_d	8.86e-30	4	218	1	208	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.
cd00761	Glyco_tranf_GTA_type	4.85e-24	4	121	1	115	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	1.37e-23	3	173	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.
COG0463	WcaA	4.81e-14	1	292	4	290	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd02525	Succinoglycan_BP_ExoA	2.14e-13	2	111	2	108	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
QNB43326.1	1.90e-250	1	336	1	336
QQR33209.1	3.67e-248	1	336	1	336
QHV48801.1	3.67e-248	1	336	1	336
QAA62069.1	3.67e-248	1	336	1	336
QAA68828.1	3.67e-248	1	336	1	336

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P61_A	6.36e-11	2	221	15	208	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
P71054	1.08e-09	2	112	7	114	Putative glycosyltransferase EpsE OS=Bacillus subtilis (strain 168) OX=224308 GN=epsE PE=2 SV=2
Q6GV29	7.51e-08	1	119	15	136	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 OS=Rattus norvegicus OX=10116 GN=B3gntl1 PE=2 SV=1
Q3U129	1.00e-07	1	119	15	136	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 OS=Mus musculus OX=10090 GN=B3gntl1 PE=2 SV=1
Q67FW5	1.36e-07	2	119	20	140	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 OS=Homo sapiens OX=9606 GN=B3GNTL1 PE=2 SV=2
A0A0H2UR96	1.42e-07	1	129	4	128	Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG 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
1.000076	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001921_01820.