CAZyme Information: EPrPVT00000013598-p1

Basic Information

• Species: Phytopythium vexans
• Lineage: Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
• CAZyme ID: EPrPVT00000013598-p1
• CAZy Family: AA1
• CAZyme Description: Mannosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
414		45945.16	4.6867

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PvexansDAOMBR484	11991	1223560	34	11957

• Gene Location: location=PvexDAOMBR484_SC0012:32981-34735(-)

Full Sequence      

MRRHLFAATLLFGGACLQVAAVPPVVLWYAPFLSGGGYSSEAHSYVKAIASALNQPSRSA
DHDAASSTADQAVSSSASSASNDGSAEQPEMEKPFVLRVTQHGDSMNPRFIDAMPEEMRE
LMEEVLSVALFQEDVFKAGGVRPEMIKIVPEAVDIQFFDPNAVEAPYDLASEVDFELTDK
TTVFLSIFKWERRKGWQVLLEAYFKAFERGDDVVLVLLTNAYHEAFDSAGDFTQVIEKFT
MSTLGKKLSELPRVHVLPPHIPQDAMPSLYKAATAFVLPSRGEGWGRPHVEAMAMELPVI
ATFWSGTTEYMTPENSYPLEINGLVEIPDGAFRGHRWADPSVEHLQKLLQQVKLHPEEAI
AKGKQARQDMLDKYSPEVIGELIFDHITRILALVRAQDKKEVDKDEAAVGHEEL

Enzyme Prediction     

No EC number prediction in EPrPVT00000013598-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	179	315	2.8e-18	0.75625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340831	GT4_PimA-like	2.99e-25	108	379	128	357	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.
340828	GT4_WlbH-like	3.60e-25	134	395	163	374	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.
223515	RfaB	1.71e-20	125	392	154	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340838	GT4_MtfB-like	9.91e-16	132	368	150	350	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.
340816	Glycosyltransferase_GTB-type	1.11e-15	146	319	79	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26988.1|GT4	2.25e-146	23	414	155	607
QTJ63792.1|GT4	5.42e-99	193	382	1	190
QTJ63791.1|GT4	5.62e-99	193	382	2	191
QTJ63793.1|GT4	1.09e-98	193	381	2	190
QTJ63794.1|GT4	3.20e-98	193	382	2	191

PDB Hits     

EPrPVT00000013598-p1 has no PDB hit.

Swiss-Prot Hits     

EPrPVT00000013598-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.003479	0.996466	CS pos: 21-22. Pr: 0.9517

TMHMM  Annotations     

Start	End
7	29