CAZyme Information: PUG3_T003036-RA-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PUG3_T003036-RA-p1
• CAZy Family: PL1
• CAZyme Description: Glycosyl transferase, group 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
431		48956.50	5.6623

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GultimumBR650	14086	1223559	0	14086

• Gene Location: location=PultBR650_SC0154:2874-4508(+)

Full Sequence      

MEETAVDEQDGYTINTLPHSHGGSSKGSQAAVSSTKYVAPFSLLVTQHGDSLNAAFIRDI
PDSMHELLKEHWIEERDFNWRLSDRKIAIAICHSEPGAWHPARYTTSRCPPKGALYKVGR
TMFETDRVPSGWPERMNNMDEIWVPTRFQEHVFIEGRVRAEAIKVVPEAVDVDFFNPEQV
ETPYDLASELAETGFTMTEHTTVYLSIFKWEERKAWRVLIKAYFEAFAPEDDVVLVLLTN
AYHVQSETAKDFLEIIDVFAREAVGKTLKKLPKLHVLPPHLPQTALPSLYKAATAFVLPS
RGEGWGRPHVEAMAMELPVIATFWSGTTEYMTEENSYRLRIDGLVEITEGAFSGHKWAEP
SINHLKELLVHVKQHPEEAIAKGKRARQDMIAKYAPDIIGDLILGHIHRILKEVARRQEQ
ETDNSEGHDEL

Enzyme Prediction     

No EC number prediction in PUG3_T003036-RA-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340828	GT4_WlbH-like	1.46e-18	158	414	170	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	5.22e-18	81	408	101	366	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	6.30e-16	137	413	149	380	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340816	Glycosyltransferase_GTB-type	1.38e-12	205	339	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	1.17e-11	286	335	67	116	Glycosyl transferases group 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26988.1|GT4	5.55e-203	29	431	209	607
VDC77730.1|GT4	4.26e-100	41	417	109	480
CAG7890560.1|GT4	4.26e-100	41	417	109	480
QTJ63794.1|GT4	4.26e-100	212	402	1	191
CAB4085108.1|GT4	1.07e-99	41	414	120	487

PDB Hits     

PUG3_T003036-RA-p1 has no PDB hit.

Swiss-Prot Hits     

PUG3_T003036-RA-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000053	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PUG3_T003036-RA-p1.