CAZyme Information: MGYG000000138_03122

Basic Information

• Species: Parabacteroides johnsonii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides johnsonii
• CAZyme ID: MGYG000000138_03122
• CAZy Family: GT2
• CAZyme Description: Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
332	MGYG000000138_12|CGC1	37683.44	9.1377

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000138	4917599	Isolate	United Kingdom	Europe

• Gene Location: Start: 121232; End: 122230 Strand: -

Full Sequence      

MATPHLSLIIPVYNRPNEVEELLDSLTRQSETNFEVVIVEDGSKETCQHVAEAFKDRLDV
SYCYIPNGGPGNARNYGAKQSKGDYLIVLDSDCILPPDYIKSVNKELEETGADAFGGPDK
ASDSFTDVQKAINYSMTSFFTTGGIRGGKKKMDKFYPRSFNMGIRKSTYEALEGFSAMRF
GEDIDFSIRLFKNGYKVCLFPSAWVYHKRRTDWRKFFRQVYNSGIARINLYKKYPDSLKL
VHLLPAVFTLGVFFFLVGSLFCTWSLLPLGLFSLLIFVDSSIQNKSLKIGFLSIIASFIQ
LIGYGCGFLDAAWNRLVLKKKEFSAFQKTFYK

Enzyme Prediction     

No EC number prediction in MGYG000000138_03122.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	7	155	2.1e-31	0.8941176470588236

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02525	Succinoglycan_BP_ExoA	4.40e-49	7	248	3	248	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	3.13e-31	7	167	1	163	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	5.33e-29	9	118	2	114	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	4.47e-25	4	219	54	276	Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
cd06420	GT2_Chondriotin_Pol_N	8.00e-24	8	207	1	180	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT49895.1	6.89e-233	1	332	1	332
QUT44705.1	1.72e-170	7	332	33	358
QRQ50314.1	2.02e-169	7	332	4	329
QPH58349.1	2.87e-169	7	332	4	329
QBJ18043.1	2.35e-168	7	332	4	329

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HEA_A	2.49e-14	6	113	7	115	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]
5TZE_C	3.20e-14	7	113	4	114	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	5.31e-14	7	113	4	114	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	2.83e-08	4	102	5	99	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]
2Z86_A	1.38e-07	4	101	375	473	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q68X33	6.79e-16	3	101	7	103	Uncharacterized glycosyltransferase RT0329 OS=Rickettsia typhi (strain ATCC VR-144 / Wilmington) OX=257363 GN=RT0329 PE=3 SV=1
Q48214	6.18e-15	6	212	2	207	Uncharacterized glycosyltransferase HI_1696 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1696 PE=3 SV=2
Q9ZDI9	1.46e-14	3	101	7	103	Uncharacterized glycosyltransferase RP339 OS=Rickettsia prowazekii (strain Madrid E) OX=272947 GN=RP339 PE=3 SV=1
Q1RIM7	3.09e-14	6	109	293	396	Uncharacterized glycosyltransferase RBE_0706 OS=Rickettsia bellii (strain RML369-C) OX=336407 GN=RBE_0706 PE=3 SV=1
Q4UM29	6.93e-14	6	109	295	398	Uncharacterized glycosyltransferase RF_0543 OS=Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) OX=315456 GN=RF_0543 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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
247	278
291	313