CAZyme Information: MGYG000000056_00965

Basic Information

• Species: Muribaculum sp002358615
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Muribaculum; Muribaculum sp002358615
• CAZyme ID: MGYG000000056_00965
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
377	MGYG000000056_6|CGC1	43238.93	8.7514

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000056	3324937	Isolate	United Kingdom	Europe

• Gene Location: Start: 20058; End: 21191 Strand: +

Full Sequence      

MILFFCIPDEVEYDGEAYFSNPISVMLNRYARSDDKVICVAPVKRVGKGSSDKICNGSVE
FQFIDKMNSFNSLLNWNVFKTRLNTIIEKCDACIIHVHSSFVSNLAFEIAHQQHKPILTV
VCGCPWDALWNYSLKGKLLAPFAYLWLKRVQQRAQYSIYVTSEFLQNRYPTCGQQINCSN
VELNTYQIDLATRYTTILSGRRFRIATVAAVDVKYKGQQYIIKALKKLRDKGIEFEYYIV
GSGNPSYLKRLTKKYQVEDLVFFTGPIKHSEIFQFLDDIDIYAQPSKQEGLPRAVIEAMS
RGCLCIGSKIAGIPELIEPEFLFRAGNISQIVDILKNIDNNVLKEQARKNVIKAQQYSKS
VLDERRSSFLNEFKNDI

Enzyme Prediction     

No EC number prediction in MGYG000000056_00965.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	207	338	2.9e-22	0.8375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	1.64e-29	94	371	85	366	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	8.25e-29	202	333	1	130	Glycosyl transferases group 1.
COG0438	RfaB	2.82e-27	94	376	86	380	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00534	Glycos_transf_1	8.64e-25	213	353	12	157	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.
cd03808	GT4_CapM-like	9.49e-25	36	354	29	347	capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKH96930.1	1.98e-121	1	376	1	378
QWI24608.1	1.53e-88	29	375	31	388
EEV38224.1	5.73e-88	24	376	26	386
QWI13766.1	2.36e-87	12	377	13	384
AVX07239.1	3.75e-83	12	373	13	380

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2JJM_A	1.39e-07	214	351	222	365	CrystalStructure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_B Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_C Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_D Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_E Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_F Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_G Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_H Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_I Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_J Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_K Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_L Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames]
3MBO_A	1.46e-07	214	351	242	385	CrystalStructure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_B Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_C Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_D Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_E Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_F Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_G Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_H Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis]
5D00_A	9.63e-06	214	329	212	328	Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39859	6.01e-37	11	348	11	344	Protein CapJ OS=Staphylococcus aureus OX=1280 GN=capJ PE=4 SV=1
Q46638	6.07e-11	173	318	197	345	Amylovoran biosynthesis glycosyltransferase AmsK OS=Erwinia amylovora OX=552 GN=amsK PE=3 SV=2
Q81ST7	7.39e-07	214	351	209	352	N-acetyl-alpha-D-glucosaminyl L-malate synthase OS=Bacillus anthracis OX=1392 GN=bshA 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
1.000031	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000056_00965.