CAZyme Information: MGYG000003132_00753

Basic Information

• Species: Dysgonomonas sp900556485
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; Dysgonomonas sp900556485
• CAZyme ID: MGYG000003132_00753
• CAZy Family: GT4
• CAZyme Description: Glycosyltransferase Gtf1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
368		43175.89	8.9513

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003132	2983269	MAG	United States	North America

• Gene Location: Start: 200514; End: 201620 Strand: +

Full Sequence      

MNNLCCIFNFAAHYRSSIYHLIDDELKADFYIGDSVGQLKAMNYHSLKGYKRSLKNVHLF
YLFNWQKGAITTVFKHYQHYLITGDFFCLSTWIVLLLCKVMQKHTYLWTHGWYGREGRIK
KWVKRVFFNLSSEVLLYGEYARGLMIKEGFNSQKLHCIANSLDYDTQLKIRNDLKKTNIY
KEHFKNNHPNLIFVGRITQIKRIDMLIEAIVCLQKQGIPVNLTLVGDPMPEFDIKSFLKN
RKLENHVWLCGACYDEHRLGEYFYNADACVSPGNVGLTSIHAFSYGCPVITHNNFSMQMP
EFEIIKNGVNGAFYEYDNLDSLTDTIHRWIEYAHDKKNNIHKNCYNIIDSKFNPHYQIAL
LKKIINKS

Enzyme Prediction     

No EC number prediction in MGYG000003132_00753.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	181	332	8.2e-17	0.93125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0438	RfaB	1.22e-20	10	367	17	376	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00534	Glycos_transf_1	4.14e-18	191	333	5	155	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
cd03801	GT4_PimA-like	1.93e-16	79	331	89	332	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
pfam13692	Glyco_trans_1_4	5.85e-16	189	331	2	137	Glycosyl transferases group 1.
cd01635	Glycosyltransferase_GTB-type	1.14e-15	192	311	114	232	glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUI56186.1	4.56e-132	2	366	5	369
QUI93286.1	4.02e-128	2	367	3	368
QCQ37686.1	1.74e-127	2	366	6	371
QCQ45080.1	1.74e-127	2	366	6	371
QLK82468.1	1.74e-127	2	366	6	371

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.999929	0.000073	0.000010	0.000000	0.000000	0.000005

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003132_00753.