CAZyme Information: MGYG000002463_05800

Basic Information

• Species: Pseudomonas aeruginosa
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas; Pseudomonas aeruginosa
• CAZyme ID: MGYG000002463_05800
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
334	MGYG000002463_68|CGC3	37777.26	8.5405

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002463	6750396	Isolate	Brazil	South America

• Gene Location: Start: 190426; End: 191430 Strand: -

Full Sequence      

MLLSVVVSTWRRPKELKLVLAGLVAQSLAFKDFEVIVVDSNSGDETPDVVREFEAVQGFN
VRLEQAELNSASAKRNKGVRLAKGRYVVLLDDDCVPDPAHLSNFLNAANSRRGERVIWCG
GVRFSCSLVSTSNYYRYRDSCHFSADKPLPNSLGYKTIVTMNMLAERDILLQDNALFDER
FVGYGFEDTEFGLRVGKLGYSVLPCRAEIEHVEPEGSISKFCRKYYHAARDGMPEFMKVA
TTDDLETLGPIRWMEPGFALSSKFQSLFRAVLCLALESKFSNILIHSLEKTDSIRWLYSR
AAYRLVLASSYRKGVLDRKSKLSKEKANKDGWYS

Enzyme Prediction     

No EC number prediction in MGYG000002463_05800.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	4	111	8.8e-23	0.6235294117647059

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06420	GT2_Chondriotin_Pol_N	4.64e-24	5	199	1	166	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.
cd00761	Glyco_tranf_GTA_type	3.52e-21	5	124	1	118	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	1.27e-19	4	170	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.
cd02525	Succinoglycan_BP_ExoA	8.03e-18	4	233	3	225	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.
cd04186	GT_2_like_c	1.21e-16	5	203	1	155	Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDR01364.1	4.22e-244	1	334	1	334
QLD77988.1	4.22e-244	1	334	1	334
AUA70245.1	4.22e-244	1	334	1	334
AVR82254.1	4.22e-244	1	334	1	334
AZN05069.1	4.22e-244	1	334	1	334

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Z87_A	4.56e-11	3	216	94	333	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	4.57e-11	3	216	95	334	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	5.61e-06	4	93	4	93	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	7.21e-06	4	93	4	93	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
Q8L0V4	2.61e-10	3	216	152	391	Chondroitin synthase OS=Escherichia coli OX=562 GN=kfoC PE=1 SV=1
D4GYH2	8.60e-10	4	200	10	195	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
Q7BLV3	9.29e-10	3	199	160	381	Hyaluronan synthase OS=Pasteurella multocida OX=747 GN=hyaD PE=1 SV=2
H2K893	1.47e-07	2	107	10	115	Validoxylamine A glucosyltransferase OS=Streptomyces hygroscopicus subsp. jinggangensis (strain 5008) OX=1133850 GN=valG PE=1 SV=1
Q15JF5	4.88e-07	2	107	41	146	Validoxylamine A glucosyltransferase OS=Streptomyces hygroscopicus subsp. limoneus OX=264445 GN=vldK 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
1.000057	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002463_05800.