CAZyme Information: MGYG000003252_01427

Basic Information

• Species: Bacteroides sp900761785
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900761785
• CAZyme ID: MGYG000003252_01427
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
179		21070.62	9.7849

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003252	8296673	MAG	United States	North America

• Gene Location: Start: 3848; End: 4387 Strand: -

Full Sequence      

MTKEKFQLPEKYLLYIGRITPKKIHRLLTYFVNYKKKYSDSTLRLVLVGGLAMERFEHPD
VIYTGFVSDEEKMSILQHADIVVNPSRYESLSLILLEAMSQKRPMLVNGHCKVLKEHCLK
SDFASFYYMNNRGFNQALRRIEQSEDLREEMGEKGVFYVKSNYNWTLIMGRLKQAIKSI

Enzyme Prediction     

No EC number prediction in MGYG000003252_01427.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	5	153	5.4e-18	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	5.56e-26	9	172	191	361	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.
cd03809	GT4_MtfB-like	1.24e-23	3	165	185	353	glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
COG0438	RfaB	1.57e-21	9	179	198	377	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd01635	Glycosyltransferase_GTB-type	8.07e-20	2	111	102	220	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.
pfam00534	Glycos_transf_1	1.10e-19	10	155	2	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAO78474.1	1.34e-123	1	179	209	387
QMW89170.1	1.34e-123	1	179	209	387
ALJ44445.1	3.14e-123	1	179	235	413
QQA08508.1	3.14e-123	1	179	235	413
BCA52681.1	5.92e-121	1	179	235	413

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q4JAK2	4.67e-07	10	179	179	351	Archaeal glycosylation protein 16 OS=Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) OX=330779 GN=agl16 PE=3 SV=1
Q65CC7	3.00e-06	61	164	266	369	Alpha-D-kanosaminyltransferase OS=Streptomyces kanamyceticus OX=1967 GN=kanE 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
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003252_01427.