CAZyme Information: KAG1703207.1

Basic Information

• Species: Phytophthora capsici
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora capsici
• CAZyme ID: KAG1703207.1
• CAZy Family: GH78
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
474		53512.24	5.1394

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcapsiciLT1534	28579	763924	5206	23373

• Gene Location: location=JADEVP010000019:499056-500626(-)

Full Sequence      

MKVLPLFFPLCVLLATPTAGFGRRPIVSNDPAPPAVLWYAPFLSGGGYCSEAHSYVVAVD
TAVGESASSSSTSEDLEVEQEEKVVEKPFELLITQHGDSLNTSFIRDLPTDMKSKLEHHW
IEERDFYWRLKNRKIALAICHSEPGAWAPAHYMTSRCPPEKAQYKVGRTMFETDRVPKGW
PDRMNKMDEIWVPTKFQEKIFVDGGVKPEAVKVVPEVVDVDFFDPEKVEKVYDLAGETAF
EMTEKTTVYLSIFKWEERKAWRVLLKAYFEAFKVEDDVVLVLLTNGYHTTSSSAEDFMGV
IEKFSLEAVGKKLDELPHIHVLPPHIPQEAMPSLYKAADAFVLPSRGEGWGRPHVEAMAM
ERPLIATFWSGTTEYMTEENSYPLEIDGLIEITEGAFKGHKWADPSVRHLTELLIRVKEH
PEEAVAKGKQARKDMVEKYSPAIIGKIVLGHITRILEHVAALEKASEAEGHEEL

Enzyme Prediction     

No EC number prediction in KAG1703207.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	244	381	3.8e-16	0.7625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340828	GT4_WlbH-like	2.27e-18	181	455	136	376	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	7.25e-18	255	452	201	365	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	7.10e-16	116	457	92	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340816	Glycosyltransferase_GTB-type	2.38e-14	250	384	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.
404563	Glyco_trans_1_4	1.34e-12	255	380	11	116	Glycosyl transferases group 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26988.1|GT4	5.56e-258	27	474	149	607
BAF24714.1|GT4	1.36e-112	33	456	76	484
BAT07314.1|GT4	1.36e-112	33	456	76	484
BAD33210.1|GT4	1.36e-112	33	456	76	484
BAG91852.1|GT4	1.36e-112	33	456	76	484

PDB Hits     

KAG1703207.1 has no PDB hit.

Swiss-Prot Hits     

KAG1703207.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000421	0.999525	CS pos: 20-21. Pr: 0.9708

TMHMM  Annotations     

There is no transmembrane helices in KAG1703207.1.