CAZyme Information: MGYG000000030_02112

Basic Information

• Species: CAG-603 sp900066105
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-603; CAG-603 sp900066105
• CAZyme ID: MGYG000000030_02112
• CAZy Family: GT8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
279		33314.54	8.4814

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000030	3025033	Isolate	United Kingdom	Europe

• Gene Location: Start: 170883; End: 171722 Strand: +

Full Sequence      

MINVLFSGNEKVFDGVLTCVLSILKRTDTKEPFRFYVYTMDATRVMPEYTPISDPLIEFL
DGIVKEYNVENSMVKVDVTELYEKEFAYCPNEQAYCSPYTLLRLFADIVPDMPDKLLYLD
VDILFNRDIRLLYDIDITEYEYAAARDHYGKYLLNPNYINAGVLLFNMKKIRKTGLLEKS
RKLIKEKKLVFADQSAVYRSTTKKKMLPQRFNDQKFLHKHTVVRHFSKRLFYLPYPHTDN
IKQWRVSDIHRVFGYYVFDDILYEYIYLKNKYERESKGD

Enzyme Prediction     

No EC number prediction in MGYG000000030_02112.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT8	3	227	1.7e-31	0.8404669260700389

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04194	GT8_A4GalT_like	3.53e-35	2	212	1	208	A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.
pfam01501	Glyco_transf_8	4.45e-17	3	194	1	197	Glycosyl transferase family 8. This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.
COG1442	RfaJ	8.05e-15	2	212	3	211	Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis].
cd00505	Glyco_transf_8	2.77e-12	15	212	15	212	Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.
cd06431	GT8_LARGE_C	8.91e-05	16	194	16	198	LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis. The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQA01162.1	6.14e-139	1	277	1	277
QNL97925.1	3.11e-133	1	277	1	277
AEE15925.1	2.45e-72	1	278	1	276
QAT42778.1	3.50e-66	3	274	2	275
ANK66321.1	2.49e-65	3	271	2	272

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P43974	1.65e-08	3	180	40	210	Putative glycosyltransferase HI_0258 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0258 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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000030_02112.