CAZyme Information: PPTG_14411-t26_2-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_14411-t26_2-p1
• CAZy Family: GH81
• CAZyme Description: hypothetical protein, variant

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
434		49145.21	6.2809

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669603:64998-66375(-)

Full Sequence      

MKVLLLFLALEALLTTPTAAFGRRPPSNNESKPPAVLWYAPFLSGGGYCSEAHSYVVAVD
AAMGMSSLSSSTTGSQGEPKSVQDTGTDSASEKPFELLITQHGDSLNPAFIRDLPEDMKA
KLEQHWIEERDFYWRLKHRKTALAICHSEPGAWEPAHYITSRCPPEGALYKVGRTMFETD
RVPRGWPERMNKMDEIWVPTKFQEKIFIDGGVRPEAVKVVPEVVDVDFFDPEKVKQVYDL
ASEVAFKMTEKTTVYLSVFKWEERKAWRVLLKAYFQAFTAEDDAVLVLLTNGYHTTSSSA
DDFMNVIEKFALEAVGKKLDELSNVHVLPPHIPQDTMPSLYKAAHAFVLPSRGEGWGRPH
VEAMAMERPVIATFWSGTTEYMTEENSYPLKIDGLIEIEEGAFKGHKWADPSVKHLKELL
LRIKEHPQVRRWKK

Enzyme Prediction     

No EC number prediction in PPTG_14411-t26_2-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	250	387	1.2e-17	0.7625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340828	GT4_WlbH-like	9.72e-17	250	387	198	320	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.
340816	Glycosyltransferase_GTB-type	4.96e-16	256	390	114	234	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.
340831	GT4_PimA-like	3.30e-15	261	432	201	339	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.
223515	RfaB	4.98e-14	125	397	95	330	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
404563	Glyco_trans_1_4	9.17e-14	261	386	11	116	Glycosyl transferases group 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26988.1|GT4	7.41e-243	28	428	150	554
BAF24714.1|GT4	4.60e-102	23	423	63	445
BAT07314.1|GT4	4.60e-102	23	423	63	445
BAD33210.1|GT4	4.60e-102	23	423	63	445
BAG91852.1|GT4	4.60e-102	23	423	63	445

PDB Hits     

PPTG_14411-t26_2-p1 has no PDB hit.

Swiss-Prot Hits     

PPTG_14411-t26_2-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000210	0.999763	CS pos: 20-21. Pr: 0.9750

TMHMM  Annotations     

There is no transmembrane helices in PPTG_14411-t26_2-p1.