CAZyme Information: MGYG000000915_02321

Basic Information

• Species: Clostridium nigeriense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium nigeriense
• CAZyme ID: MGYG000000915_02321
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
340	MGYG000000915_8|CGC7	38944.61	9.8378

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000915	3503945	MAG	China	Asia

• Gene Location: Start: 138300; End: 139322 Strand: +

Full Sequence      

MNKTVSIIIPCRNEENYIKQCIDSFLNQSYPKELIEIIIADGMSTDNTRNIINEISKKNT
NVVLIDNKKFTAPAGMNIGIKKSRSDIIIIFGAHAYADKDFVKENVLALKNDDIGCTGGL
INTINDSIKGEAIAEAMSCPFGVGNALFRYADKEAFVDTVGFGAYDRQFIIDIGLFDEEL
VRNQDDELNFRVQKSGKKILLNPRIKATYFSRGDFKKLWKQYYQYGFWKVRVIQKHKKPA
SIRHLIPLMFVLFLLFGGIASIFSSLIRIGYFLTIILYLALDAMFSVKICRKKSFSHFPY
LFITFPILHISYGIGFILGLFNFYIFKSKKMEEKNKQISR

Enzyme Prediction     

No EC number prediction in MGYG000000915_02321.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	6	129	1.6e-26	0.7235294117647059

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02525	Succinoglycan_BP_ExoA	3.25e-113	4	251	1	249	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.
pfam00535	Glycos_transf_2	1.42e-23	6	167	1	161	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.
COG1215	BcsA	4.89e-23	3	326	54	400	Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
cd00761	Glyco_tranf_GTA_type	3.30e-22	7	199	1	153	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.
cd06423	CESA_like	9.39e-22	7	179	1	175	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SNV86342.1	3.77e-149	4	340	8	343
ABK61229.1	4.99e-149	4	340	6	341
VTQ94426.1	1.89e-148	1	340	1	339
AVP53972.1	6.20e-148	4	340	8	343
AAO36740.1	6.20e-148	4	340	8	343

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P61_A	1.87e-16	4	194	14	185	Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]
5TZE_C	3.31e-08	6	104	4	103	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]
5HEA_A	3.32e-08	5	148	7	162	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]
5TZ8_A	4.52e-08	6	104	4	103	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]
3BCV_A	3.40e-06	5	100	7	100	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B3VA59	1.87e-46	5	319	4	316	Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase OS=Methanococcus voltae OX=2188 GN=aglC PE=1 SV=1
P33691	2.13e-20	7	323	13	325	Succinoglycan biosynthesis protein ExoA OS=Rhizobium meliloti (strain 1021) OX=266834 GN=exoA PE=3 SV=1
D4GYH2	2.27e-16	5	226	9	224	Glycosyltransferase AglI OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=aglI PE=1 SV=1
P96587	5.78e-13	5	259	51	317	Uncharacterized glycosyltransferase YdaM OS=Bacillus subtilis (strain 168) OX=224308 GN=ydaM PE=3 SV=1
E0U4V7	4.73e-11	5	105	3	112	Poly(ribitol-phosphate) beta-glucosyltransferase OS=Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) OX=655816 GN=tarQ PE=1 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
1.000060	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
245	267
269	287
302	324