CAZyme Information: MGYG000000022_01980

Basic Information

• Species: Faecalibacterium prausnitzii_C
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_C
• CAZyme ID: MGYG000000022_01980
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
342	MGYG000000022_6|CGC1	39033.89	7.9915

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000022	3052239	Isolate	United Kingdom	Europe

• Gene Location: Start: 6373; End: 7401 Strand: +

Full Sequence      

MAQKLITFAVPCYNSAAYMRHCIETLLSAGEQAEIILVDDGSTKDDTPAICDEYAAKYPT
IVKAIHQENGGHGEGVNQGIRNATGLYYKVVDSDDWLDEAALRTVLAKLNTLTARGTAPD
LMICNYVYEHVEDNTSHTVRYTNVFPQNRLFSWTHVGHFRPDQNLLMHSVMYRTQVLRDC
GMVLPKHTFYVDNIFVYQPLPFVKSMYYMDLDLYRYFIGRADQSVNESVMVKRVDQQLRV
TRHMIDCQDLDALKGQKKLRSYMLHYLSMMMAISDIFLLLDGSAAAKQKENELWAYLKAH
TSAGVYRSIRYGFGGVTNLKIPKGDKLVLGGYRLAQKIFKFN

Enzyme Prediction     

No EC number prediction in MGYG000000022_01980.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	9	164	2.3e-27	0.9117647058823529

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00761	Glyco_tranf_GTA_type	1.17e-23	10	109	3	102	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.
pfam00535	Glycos_transf_2	7.45e-23	7	168	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.
COG0463	WcaA	1.37e-22	3	218	2	210	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
PRK10073	PRK10073	5.76e-19	10	245	12	240	putative glycosyl transferase; Provisional
cd04179	DPM_DPG-synthase_like	4.80e-17	10	94	3	89	DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATP00344.1	5.02e-256	1	342	1	342
QIA43928.1	5.02e-256	1	342	1	342
ATL90515.1	3.25e-252	1	342	1	342
AXA82374.1	4.79e-229	1	342	1	342
CBK99603.1	2.77e-228	1	342	1	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3BCV_A	1.37e-17	6	98	7	98	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	2.77e-11	5	106	375	475	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	2.78e-11	5	106	376	476	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]
5TZE_C	4.47e-08	10	125	7	144	Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
5TZ8_A	6.10e-08	10	125	7	144	Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P71057	1.56e-16	1	129	1	122	Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 SV=1
A0A0H2URH7	6.54e-13	1	144	2	148	Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
P71059	1.46e-11	5	137	4	129	Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
Q4UM29	1.48e-11	5	232	15	216	Uncharacterized glycosyltransferase RF_0543 OS=Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) OX=315456 GN=RF_0543 PE=3 SV=1
Q9ZDI9	1.34e-10	3	139	7	133	Uncharacterized glycosyltransferase RP339 OS=Rickettsia prowazekii (strain Madrid E) OX=272947 GN=RP339 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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000022_01980.