CAZyme Information: EPrPAT00000016382-p1

Basic Information

• Species: Pythium aphanidermatum
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
• CAZyme ID: EPrPAT00000016382-p1
• CAZy Family: CE5
• CAZyme Description: Alpha-1,3-mannosyltransferase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
445		49276.16	8.7796

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444	12363	1223555	58	12305

• Gene Location: location=PaphDAOMBR444_SC0096:56833-58170(+)

Full Sequence      

MELITGVALLALLVVVLGVRTLYAFYIGLTLSTSALRRPLPKRPLRIGFVHPDFGIGGAE
NLVVNAAIALQKSGAQVEIFTAHHDVSHCFEETRGDGPLARCVRVHGDWLPKTIAGKLYA
FCAILRILYVTLVISITYADEIDAFFVDQVSVSIPFLRFMGKPVLFYGHYPDKLLVIKSK
SKLKALYRWPLDTLEEITTACSDVIVVNSEFTRSVFQQSFRSLQKRELGVLYPPVDVSVF
ERFEASSPRNPSQFVSLNRFERKKNVALAIHALAKLKSLVSADVFDSTRLIIAGGYDPNN
KENIEHLKELQQEVTKYSLQKHVEFRTSVSDSMKKELLSTSAAILYTPDKEHFGIVPVEA
MTCRTPVIAVASGGPLESIKDDHTGFLCKAEPDAFACAMAKVCGPSKSTRVSDMGENGRE
RARALFSLEAFANSLYKSVGSMFTK

Enzyme Prediction     

EC	2.4.1.257:6	2.4.1.132:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	249	402	1e-36	0.88125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340834	GT4_ALG2-like	0.0	45	435	1	392	alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
340831	GT4_PimA-like	7.20e-41	46	437	1	363	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	2.66e-36	45	437	3	372	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340835	GT4_ALG11-like	5.95e-35	47	434	3	419	alpha-1,2-mannosyltransferase ALG11 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.
215511	PLN02949	2.43e-32	22	444	7	459	transferase, transferring glycosyl groups

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ22829.1|GT4	4.94e-185	15	439	17	443
CCA25726.1|GT4	2.04e-164	2	436	6	442
AAH92211.1|GT4	5.18e-117	49	439	7	399
AAH49444.1|GT4	7.44e-116	45	442	22	420
AAI51889.1|GT4	1.56e-115	45	442	2	400

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6KIH_A	1.61e-15	228	432	225	414	Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus]
2F9F_A	4.60e-09	254	402	26	159	Crystal Structure of the Putative Mannosyl Transferase (wbaZ-1)from Archaeoglobus fulgidus, Northeast Structural Genomics Target GR29A. [Archaeoglobus fulgidus DSM 4304]
3C4Q_A	5.10e-07	183	435	138	398	Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum]
3C48_A	5.21e-07	183	435	158	418	Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum]
2JJM_A	1.11e-06	176	439	139	381	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94738|ALG2_RHIPU	1.60e-103	40	435	1	416	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Rhizomucor pusillus OX=4840 GN=ALG2 PE=1 SV=1
sp|Q9DBE8|ALG2_MOUSE	1.68e-101	49	439	19	411	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Mus musculus OX=10090 GN=Alg2 PE=1 SV=2
sp|Q9H553|ALG2_HUMAN	3.90e-100	49	439	19	411	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Homo sapiens OX=9606 GN=ALG2 PE=1 SV=1
sp|Q96WW6|ALG2_SCHPO	7.21e-90	32	441	4	425	Alpha-1,3/1,6-mannosyltransferase alg2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg2 PE=3 SV=2
sp|Q7KWM5|ALG2_DICDI	1.89e-86	42	435	5	413	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Dictyostelium discoideum OX=44689 GN=alg2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000032	0.000000

TMHMM  Annotations     

Start	End
7	29