CAZyme Information: MGYG000004797_01785

Basic Information

• Species: Phocaeicola sartorii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sartorii
• CAZyme ID: MGYG000004797_01785
• CAZy Family: GT4
• CAZyme Description: Glycosyltransferase Gtf1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
326	MGYG000004797_21|CGC1	38286.47	7.6099

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004797	5247182	MAG	China	Asia

• Gene Location: Start: 58878; End: 59858 Strand: -

Full Sequence      

MKIFSINTELDKVTGVQKVLVDIHCAVKDKYVAKIVSQLSYRQIDSNLRIQEEEYICWRN
PFLFYNSLVFVHERKVLLILWLLNTLLFQRIKIIYIHHNILRGWRWVPMPKCVVAISDRC
LDNLLNYFNLNPRHIHKIYNCVNDIHPFSHKYKEGLEIKVLYPARINGVKRQIEIVNYLK
GRLSPYVKILFAGTGPSYEELNNITKENSQFITLGFRNDILQLFQQCDYVLLFSEHEGLP
ITLIEATMCGTPIVCNDVGGNCEIAYDGENAIVVNEWEKLIETLNKLPEISEVEYRRMSN
ASRNIYEKNFTFEAFKQNYLNLLNEL

Enzyme Prediction     

No EC number prediction in MGYG000004797_01785.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	159	298	6.5e-22	0.91875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03801	GT4_PimA-like	4.31e-34	50	324	71	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.
cd03808	GT4_CapM-like	1.49e-27	95	313	124	351	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.
COG0438	RfaB	1.01e-22	90	326	131	377	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03811	GT4_GT28_WabH-like	5.93e-22	90	282	105	318	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.
cd03819	GT4_WavL-like	5.30e-21	90	264	99	293	Vibrio cholerae WavL and similar sequences. This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALK84634.1	2.54e-123	2	326	14	339
QBQ39828.1	2.72e-79	1	326	4	331
QEC79472.1	3.42e-72	1	326	3	332
AYL95783.1	1.53e-70	1	323	3	329
QTE60401.1	3.30e-66	1	326	3	332

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2JJM_A	4.26e-08	107	308	154	368	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	4.43e-08	107	308	174	388	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]
6N1X_A	5.46e-08	107	275	143	322	ChainA, Glycosyltransferase [Staphylococcus aureus subsp. aureus CN1]
6D9T_A	5.75e-08	107	275	159	338	BshAfrom Staphylococcus aureus complexed with UDP [Staphylococcus aureus]
4XYW_A	1.55e-07	137	287	159	305	GlycosyltransferasesWbnH [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q0P9C9	2.20e-08	168	319	217	369	N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglA PE=1 SV=1
Q81ST7	2.26e-07	107	308	141	355	N-acetyl-alpha-D-glucosaminyl L-malate synthase OS=Bacillus anthracis OX=1392 GN=bshA PE=1 SV=1
P0DMP6	8.51e-07	137	287	159	305	O-antigen biosynthesis glycosyltransferase WbnH OS=Escherichia coli OX=562 GN=wbnH PE=1 SV=1
P0DMP7	8.51e-07	137	287	159	305	Probable O-antigen biosynthesis glycosyltransferase WbiN OS=Escherichia coli OX=562 GN=wbiN PE=3 SV=1
P42982	2.25e-06	151	319	190	366	N-acetyl-alpha-D-glucosaminyl L-malate synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=bshA PE=1 SV=2

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
0.999685	0.000279	0.000025	0.000002	0.000001	0.000026

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004797_01785.