CAZyme Information: EPrPRT00000019913-p1

Basic Information

• Species: Pythium arrhenomanes
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
• CAZyme ID: EPrPRT00000019913-p1
• CAZy Family: GH5
• CAZyme Description: Glycosyltransferase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
317		36126.72	4.8469

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531	13857	1223556	52	13805

• Gene Location: location=ParrATCC12531_SC01124:9014-10207(+)

Full Sequence      

EANSYVEAIDWAIRARRDHDARELQQKKEHEAVETERLFGLYITQHGDSYNAAFIRDLPD
PMRELLNEHWIEERDFHWRLKSTQVALAICHSEPGAWYPAHYTTSRCPPERALGWSDRMN
AMDEIWVPTKFQHQVFVDGGVRAESLHVLPEAVDVHFFDPATVDTPYDLASEITGERTIT
ASTTVFLSVFKWEERKGWKVLLRAYFAAFAASDDVVLVILTSAYHASSESAADFMAIIEA
FAQTEFDKPLRELPLVYVVPPQLPQHQLPALYKAATAFVLPSRGEGWGRPHVEAMAMGLP
IISTFWSGTTEYMTEEN

Enzyme Prediction     

No EC number prediction in EPrPRT00000019913-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	183	315	2.9e-16	0.73125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340828	GT4_WlbH-like	4.82e-21	140	317	169	319	Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
340831	GT4_PimA-like	5.44e-17	87	316	109	309	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
340838	GT4_MtfB-like	3.20e-15	140	302	158	297	glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
223515	RfaB	3.78e-15	69	317	95	319	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340816	Glycosyltransferase_GTB-type	6.81e-13	155	317	85	230	glycosyltransferase family 1 and related proteins with GTB topology. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26988.1|GT4	2.32e-131	1	317	173	512
AAG51382.1|GT4	2.53e-65	39	317	30	316
AEE74936.1|GT4	2.31e-64	39	317	119	405
AAM20561.1|GT4	2.31e-64	39	317	119	405
AAF76369.1|GT4	2.31e-64	39	317	119	405

PDB Hits     

EPrPRT00000019913-p1 has no PDB hit.

Swiss-Prot Hits     

EPrPRT00000019913-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000036	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EPrPRT00000019913-p1.