CAZyme Information: MGYG000000170_02489

Basic Information

• Species: Alistipes_A sp900240235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900240235
• CAZyme ID: MGYG000000170_02489
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
373	MGYG000000170_12|CGC1	42186.7	7.82

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000170	3119069	Isolate	China	Asia

• Gene Location: Start: 28703; End: 29824 Strand: -

Full Sequence      

MTKTRLLIVAHSGYMGGAETVLAHAINNVLSDSSRYETDVYYPLGTGSLFRTALRSETVR
RCCALPYRNIASGSLKTLIVLLYSLPTILWLIAVCLFRKTDRIYVNSAVNFPGAWVAYIT
GKRCLWHIHEQPNAHTDYLPRWMISTYRKLFTASNITPVFVTERCRRLWSQKLACDFPVY
RIAYPPLKELPLTVSKKTGTALTIGYLGALIPGKNVAALVRSYARLHTSHPQDPPYLLIC
GSGPCLHELQDLARTLHVETFTEFRAFQNDVSGFFADIDMLVQPSLNESWGLTVLEAMSQ
RKAVITTTETGLHEILTGEECLFFDPSDEDELYKCLEALQEEGLRNRLSSNGYDKVRLLN
LNHQFELTIKDIL

Enzyme Prediction     

No EC number prediction in MGYG000000170_02489.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	203	345	2e-26	0.9

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	3.49e-29	5	357	1	349	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.
cd03811	GT4_GT28_WabH-like	9.58e-29	5	351	1	337	family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
COG0438	RfaB	9.68e-23	5	357	4	358	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00534	Glycos_transf_1	1.17e-21	204	353	5	156	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.
pfam13692	Glyco_trans_1_4	1.09e-20	203	339	3	135	Glycosyl transferases group 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA22786.1	6.89e-281	1	373	1	373
AEE96555.1	8.03e-15	201	372	189	357
AFK87068.1	1.55e-14	128	356	115	350
ALT69529.1	2.49e-14	206	352	197	338
BCS54961.1	5.10e-14	200	333	186	318

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6N1X_A	1.76e-08	214	351	213	349	ChainA, Glycosyltransferase [Staphylococcus aureus subsp. aureus CN1]
6D9T_A	1.87e-08	214	351	229	365	BshAfrom Staphylococcus aureus complexed with UDP [Staphylococcus aureus]
2JJM_A	1.02e-07	214	373	224	386	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	1.07e-07	214	373	244	406	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]
4S0V_A	1.25e-06	88	340	181	435	Crystalstructure of the human OX2 orexin receptor bound to the insomnia drug Suvorexant [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q4JSW2	1.89e-07	204	328	226	361	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium jeikeium (strain K411) OX=306537 GN=mshA PE=3 SV=1
A7TZT2	2.69e-07	207	359	256	418	Mannosylfructose-phosphate synthase OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=mfpsA PE=1 SV=1
Q81ST7	5.43e-07	214	373	211	373	N-acetyl-alpha-D-glucosaminyl L-malate synthase OS=Bacillus anthracis OX=1392 GN=bshA PE=1 SV=1
C4LLD6	8.33e-07	201	354	251	413	D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717) OX=645127 GN=mshA PE=3 SV=1
D3Q051	1.93e-06	201	363	242	415	D-inositol 3-phosphate glycosyltransferase OS=Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 / LLR-40K-21) OX=446470 GN=mshA PE=3 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
1.000062	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
70	92