CAZyme Information: PHYSODRAFT_470795-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_470795-t26_1-p1
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
459	JH159151|CGC14	51467.60	5.0306

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159151:5120475-5122063(+)

Full Sequence      

MKVALLFPALCALLATPAVASGRHASVSSESGRPAVLWYAPFLSGGGYCSEAHSYVVAVD
AALGESTAMEPPFELLITQHGDSLNPSFIRDLPEDMRSKLEHHWIEERDFYWRLKNRKIA
LAICHSEPGAWEPAHYMTSRCPPEKAQYKVGRTMFETDRVPKGWPERMNKMDEIWVPTKF
QEKVFVDGGVRPEAVKVVPEVVDVDFFDPDKVEQVYDLASETAFEMTDKTTVYLSIFKWE
ERKAWKVLLTAYFEAFSVEDEVVLVLLTNGYHTSSSSAGDFQSLIEKFASEAVDKPLSEL
PHVHVLPPHISQEAMPSLYKAANAFVLPSRGEGWGRPHVEAMAMERPVIATFWSGTTEYM
TEENSYPLQIDGLIEITEGAFCGHMWADPSVKHLKELLIRVKEHPEEAVAKGKHARDDMV
AKYSPEIIGEIVLGHITRILEHVAAKEEATQSAGAHEEL

Enzyme Prediction     

No EC number prediction in PHYSODRAFT_470795-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	228	364	1.8e-16	0.75625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340831	GT4_PimA-like	2.29e-16	239	436	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	2.94e-16	100	441	92	379	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340828	GT4_WlbH-like	2.74e-15	165	439	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.
340816	Glycosyltransferase_GTB-type	4.48e-12	234	368	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.
395425	Glycos_transf_1	8.36e-12	299	418	56	158	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26988.1|GT4	3.27e-260	24	459	146	607
ACF83309.1|GT4	1.32e-114	34	448	82	499
BAF24714.1|GT4	7.32e-114	22	440	64	484
BAT07314.1|GT4	7.32e-114	22	440	64	484
BAD33210.1|GT4	7.32e-114	22	440	64	484

PDB Hits     

PHYSODRAFT_470795-t26_1-p1 has no PDB hit.

Swiss-Prot Hits     

PHYSODRAFT_470795-t26_1-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000268	0.999738	CS pos: 20-21. Pr: 0.9800

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_470795-t26_1-p1.