CAZyme Information: MGYG000001377_00802

Basic Information

• Species: Dysgonomonas mossii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas mossii
• CAZyme ID: MGYG000001377_00802
• CAZy Family: GT11
• CAZyme Description: O-antigen biosynthesis glycosyltransferase WbnK

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
291	MGYG000001377_2|CGC5	33836.5	7.3142

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001377	3951269	Isolate	not provided	not provided

• Gene Location: Start: 101233; End: 102108 Strand: +

Full Sequence      

MVTVLLSGGLGNQMFQYAAAKSLAIRLNTALSVDLYTFSKKTQATVRPYELGIFNIEDVV
ETSSLKAKAVIKARPFIQRHRSFFQRFGVFTDTYAILYQPTFEALTGGVIMSGYFQNESY
FKNISELLRKDFSFKYPLIGENKDVAGQISENQSVAVHIRRGDYLNKNSQSNFAILEKDY
YEKAINYISAHVKNPEFYVFSEDFDWIKDNLNFKEFPVTFIDWNKGKDSYIDMQLMSLCK
HNIIANSSFSWWSAWLNNSEERKIVAPERWFVDEQKNELLDCFYPQGWIKI

Enzyme Prediction     

No EC number prediction in MGYG000001377_00802.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT11	1	291	4.1e-76	0.9963768115942029

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11301	Fut1_Fut2_like	8.10e-65	1	278	1	263	Alpha-1,2-fucosyltransferase. Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer of alpha-L-fucose to the terminal beta-D-galactose residue of glycoconjugates via an alpha-1,2-linkage, generating carbohydrate structures that exhibit H-antigenicity for blood-group carbohydrates. These structures also act as ligands for morphogenesis, the adhesion of microbes, and metastasizing cancer cells. Fut1 is responsible for producing the H antigen on red blood cells. Fut2 is expressed in epithelia of secretory tissues, and individuals termed "secretors" have at least one functional copy of the gene; they secrete H antigen which is further processed into A and/or B antigens depending on the ABO genotype. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.
pfam01531	Glyco_transf_11	9.66e-30	1	291	32	297	Glycosyl transferase family 11. This family contains several fucosyl transferase enzymes.
cd11548	NodZ_like	6.46e-07	7	260	7	284	Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ. Bradyrhizobium NodZ is an alpha 1,6-fucosyltransferase involved in the biosynthesis of the nodulation factor, a lipo-chitooligosaccharide formed by three-to-six beta-1,4-linked N-acetyl-d-glucosamine (GlcNAc) residues and a fatty acid acyl group attached to the nitrogen atom at the non-reducing end. NodZ transfers L-fucose from the GDP-beta-L-fucose donor to the reducing residue of the chitin oligosaccharide backbone, before the attachment of a fatty acid group. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIK54209.1	5.33e-97	1	291	1	290
QIK59648.1	8.70e-96	1	291	1	290
ADE13114.1	2.08e-68	1	291	1	292
QTL97698.1	2.90e-67	1	291	1	274
QDC79075.1	3.14e-62	1	291	1	293

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q58YV9	3.60e-35	6	279	5	294	O-antigen biosynthesis glycosyltransferase WbnK OS=Escherichia coli OX=562 GN=wbnK 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
1.000064	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001377_00802.