CAZyme Information: MGYG000000208_00558

Basic Information

• Species: Eubacterium_G ventriosum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_G; Eubacterium_G ventriosum
• CAZyme ID: MGYG000000208_00558
• CAZy Family: GT27
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
266	MGYG000000208_2|CGC3	31166.71	7.4739

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000208	2760783	Isolate	China	Asia

• Gene Location: Start: 152958; End: 153758 Strand: +

Full Sequence      

MKKASVIIPVYNQLFSLLLVLQGFAKQSIETDEFEIIIVNDGSKDITPDTEKLFESIVSN
CMVIHTPNYGRAFARNIGINAASTNILIFNDADRIPSSNFVEKHIMHHNEGRKIVVGNPQ
NFWGEICWESNIQDEILRKKARNSIYYNEINTKINMKPENVKYIWMSLLIGNASINKKII
CDAGKFDVQFKEWGFEHFELGFRLWRQGNNIYHDSSIINYHLVHSREKNFYKSRVIENFK
IMEEKYDYDFSEEKSFLMAIVQKKYV

Enzyme Prediction     

No EC number prediction in MGYG000000208_00558.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT27	5	243	1.3e-22	0.8338983050847457

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00761	Glyco_tranf_GTA_type	2.40e-18	6	122	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.
pfam00535	Glycos_transf_2	4.35e-17	5	116	1	111	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.
cd06420	GT2_Chondriotin_Pol_N	1.03e-16	6	222	1	181	N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase. Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.
cd06423	CESA_like	5.14e-15	6	134	1	131	CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.
cd02525	Succinoglycan_BP_ExoA	7.36e-14	3	228	1	212	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AJQ26617.1	3.36e-38	4	235	21	258
QTB15740.1	5.37e-38	3	238	2	245
AJQ26587.1	1.79e-34	4	246	9	258
ACL76163.1	2.49e-34	1	224	1	228
UAC47734.1	5.67e-33	2	229	6	248

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z87_A	9.84e-13	5	208	95	315	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	9.85e-13	5	208	96	316	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]
5HEA_A	5.98e-08	5	122	8	124	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O06483	5.06e-15	3	224	2	256	Uncharacterized glycosyltransferase YfnE OS=Bacillus subtilis (strain 168) OX=224308 GN=yfnE PE=3 SV=2
Q8L0V4	5.58e-12	5	208	153	373	Chondroitin synthase OS=Escherichia coli OX=562 GN=kfoC PE=1 SV=1
H2K893	8.54e-11	5	208	12	228	Validoxylamine A glucosyltransferase OS=Streptomyces hygroscopicus subsp. jinggangensis (strain 5008) OX=1133850 GN=valG PE=1 SV=1
Q15JF5	2.19e-10	5	208	43	259	Validoxylamine A glucosyltransferase OS=Streptomyces hygroscopicus subsp. limoneus OX=264445 GN=vldK PE=3 SV=1
P71057	8.81e-08	5	118	7	118	Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 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
0.862394	0.136537	0.000477	0.000204	0.000141	0.000248

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000208_00558.