CAZyme Information: evm.model.AC2VRR_s00089g126-p1

Basic Information

• Species: Albugo candida
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo candida
• CAZyme ID: evm.model.AC2VRR_s00089g126-p1
• CAZy Family: GH32
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
258		28563.36	5.8780

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Acandida2VRR	15896	911350	72	15824

• Gene Location: location=Acan2VRR_SC089:264704-265480(+)

Full Sequence      

MPPSNPPDASPGAIITIVVISRLVYRKGMSILVQAIPIVCARTHNVRFLIGGDGPKLIDL
EQMRERYQLHDRVELLGAVPHSQVRQILCRGHIFLNSSLTESFCIAILEAASCGLYVVST
CVGGIPEVLPNDMIEFATEITGEALADAVLRAVPRASTIDRQVFHERVAKMYNWQDVAAR
TEKVYTRLCTLPDPPLIRRLQLYYGIGPIAGALACIIAAILHLYLAVLEIWYPRDTIEIA
LDYPCPNIVPESDEIHAE

Enzyme Prediction     

EC	2.4.1.198:26

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	16	152	7.7e-33	0.85625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340827	GT4_PIG-A-like	1.07e-108	5	218	185	398	phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
340831	GT4_PimA-like	2.26e-31	15	185	193	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	1.10e-30	12	189	197	378	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
404563	Glyco_trans_1_4	4.51e-27	16	151	3	134	Glycosyl transferases group 1.
395425	Glycos_transf_1	3.64e-24	15	152	3	149	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
CCA24351.1|GT4	2.16e-169	1	258	220	481
CCA23313.1|GT4	2.16e-169	1	258	220	481
UIZ23523.1|GT4	6.85e-105	15	243	59	287
QHO28314.1|GT4	1.16e-74	15	248	200	432
QHN93976.1|GT4	3.26e-74	15	248	200	432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2JJM_A	9.65e-09	45	140	241	334	Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_B Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_C Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_D Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_E Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_F Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_G Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_H Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_I Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_J Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_K Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_L Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames]
3MBO_A	9.97e-09	45	140	261	354	Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_B Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_C Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_D Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_E Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_F Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_G Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_H Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis]
5D00_A	2.28e-08	47	188	233	375	Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168]
3OKA_A	2.51e-06	21	157	205	354	Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum],3OKA_B Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum]
3OKC_A	2.56e-06	21	157	205	354	Crystal structure of Corynebacterium glutamicum PimB' bound to GDP (orthorhombic crystal form) [Corynebacterium glutamicum],3OKP_A Crystal structure of Corynebacterium glutamicum PimB' bound to GDP-Man (orthorhombic crystal form) [Corynebacterium glutamicum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q94BX4|PIGA_ARATH	2.56e-71	14	242	200	427	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Arabidopsis thaliana OX=3702 GN=PIGA PE=2 SV=1
sp|P87172|GPI3_SCHPO	1.99e-69	7	242	181	419	Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gpi3 PE=3 SV=1
sp|Q64323|PIGA_MOUSE	4.16e-61	13	247	225	462	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Mus musculus OX=10090 GN=Piga PE=2 SV=1
sp|P37287|PIGA_HUMAN	6.70e-59	15	247	226	461	Phosphatidylinositol N-acetylglucosaminyltransferase subunit A OS=Homo sapiens OX=9606 GN=PIGA PE=1 SV=1
sp|A6ZW78|GPI3_YEAS7	9.73e-54	15	254	203	448	Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit OS=Saccharomyces cerevisiae (strain YJM789) OX=307796 GN=SPT14 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

Start	End
206	228