CAZyme Information: MGYG000003842_00198

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R
• CAZyme ID: MGYG000003842_00198
• CAZy Family: GT2
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
376		43932.21	9.0674

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003842	1754576	MAG	United States	North America

• Gene Location: Start: 33234; End: 34364 Strand: +

Full Sequence      

MSNIKVSVIIPVYNAERFLEKCLESVVNQSLSDIEIICVDDGSTDRSLEILKRFQQNDSR
IKILTQQNKFAGVARNNGIKNASGKYFVFWDSDDFFEKNALEVLYNSCEKTGADICLCGA
YNYDSETGGKSEDQTFLKKRFLPKSKVFSKKTCPEYIFNIASNVPWQRMFRADFIRSHGI
EFQALPKANDTYFVMTAMYFAEKITYIEKPLINYRTNNSLSITGTASKNPLCAYDSYMAV
YEMLKKENPDERVWQSFYNRLLSGLFRSVLLQTTEDGIRTVYDKIKNEGISAFGINQHLE
REYYYFQKEFDDLNVMLNHSFAEYLMYKYKKENRDKLFYKNQAEKKLSVRLARKISRFVS
ADSKLFEIGKRILHFK

Enzyme Prediction     

No EC number prediction in MGYG000003842_00198.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	7	149	2.8e-38	0.8411764705882353

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK10073	PRK10073	7.80e-44	1	250	1	252	putative glycosyl transferase; Provisional
pfam00535	Glycos_transf_2	7.81e-40	7	171	1	160	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd00761	Glyco_tranf_GTA_type	5.74e-36	8	123	1	117	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
cd02525	Succinoglycan_BP_ExoA	4.48e-29	5	116	1	114	ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.
cd06433	GT_2_WfgS_like	1.90e-28	7	216	1	195	WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUN13096.1	7.63e-108	1	334	1	335
QUF80659.1	1.67e-93	1	328	1	327
CDG65559.1	5.71e-71	2	323	3	323
CBL24268.1	2.14e-68	1	324	1	325
SEH98465.1	8.89e-68	5	288	5	288

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HEA_A	2.16e-27	6	126	7	127	CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
3BCV_A	7.15e-21	5	119	6	120	Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
2Z87_A	6.01e-19	6	117	376	487	Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli],2Z87_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli]
2Z86_A	6.02e-19	6	117	377	488	Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_C Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_D Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli]
6H1J_A	1.46e-18	5	252	21	267	ChainA, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P71057	4.61e-32	1	290	1	287	Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 SV=1
A0A0H2URH7	2.28e-28	5	215	6	216	Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
P71059	4.20e-28	6	221	5	219	Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
A0A0H2UR96	9.41e-27	6	128	5	128	Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1
P11290	2.60e-25	2	248	4	250	Uncharacterized glycosyltransferase YibD OS=Escherichia coli (strain K12) OX=83333 GN=yibD PE=3 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
1.000039	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003842_00198.