CAZyme Information: MGYG000001193_00714

Basic Information

• Species: UBA4285 sp900545225
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA4285; UBA4285 sp900545225
• CAZyme ID: MGYG000001193_00714
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
344	MGYG000001193_3|CGC1	39273.92	9.795

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001193	1467080	MAG	Austria	Europe

• Gene Location: Start: 35100; End: 36134 Strand: +

Full Sequence      

MFITFCIFAYNEEMYLPNLLKCLRRQDYPHENIEVLLIDSMSKDSTKAMMEKFALLNNED
VADMGFRNVKVCSNPGVTQPCAWNVALDNYSGEALLRVDAHSEIPSDFIRKNVEKLEAGE
YVCGGPRPVITKSRGGMSRTVLMAETSKFGAGIAPYRNKHNSSKPKYVTSLFHAAFRREV
FDKVGRYNEKLIRTEDNDMNYRIRKAGFKLAYYDDIISYQVIRPNLFGSIKQKYDNGYWI
GKTLFVNPKCIRPFHLAPLAFLTTVVSAFMMYRMTKSEYARKLLMLVCKSYVGMAIVMSL
SAMIKNRRDFNITTLLLPFIFGAMHVAYGLGSAVGIIKGFLERK

Enzyme Prediction     

No EC number prediction in MGYG000001193_00714.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	5	185	2.8e-23	0.9882352941176471

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02525	Succinoglycan_BP_ExoA	1.03e-85	2	262	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.
cd00761	Glyco_tranf_GTA_type	1.57e-16	7	213	3	156	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.
COG1215	BcsA	2.78e-15	2	233	55	277	Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
cd06423	CESA_like	3.99e-15	9	196	5	180	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.
pfam00535	Glycos_transf_2	9.83e-15	4	181	1	164	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR71118.1	3.12e-104	1	336	1	340
QGS07417.1	1.23e-99	1	344	1	328
ASM68836.1	5.42e-95	1	338	1	323
SQH54677.1	2.32e-94	1	344	1	328
QWQ39049.1	1.14e-91	1	344	1	331

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YV7_A	1.04e-07	3	222	45	249	MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6YV7_B	1.04e-07	3	222	44	248	MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
5TZE_C	1.42e-06	9	115	9	102	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	1.87e-06	9	115	9	102	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]
6P61_A	2.34e-06	3	109	15	110	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B3VA59	9.33e-17	2	339	3	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	4.48e-11	11	261	19	262	Succinoglycan biosynthesis protein ExoA OS=Rhizobium meliloti (strain 1021) OX=266834 GN=exoA PE=3 SV=1
D4GYH2	1.03e-07	9	233	15	220	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
D4GYG7	1.49e-06	2	233	7	219	Glycosyltransferase AglE OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=aglE 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
0.999607	0.000407	0.000005	0.000001	0.000000	0.000001

TMHMM  Annotations     

start	end
254	271
283	304
319	341