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CAZyme Information: EPrPIT00000015563-p1

You are here: Home > Sequence: EPrPIT00000015563-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Globisporangium irregulare
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
CAZyme ID EPrPIT00000015563-p1
CAZy Family AA17
CAZyme Description Alpha-1,3-mannosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
454 50329.44 7.1631
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486 13869 1223557 65 13804
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.257:6 2.4.1.132:6

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 259 418 2.2e-40 0.91875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
340834 GT4_ALG2-like 0.0 56 446 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 5.22e-44 57 451 1 366
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.
340835 GT4_ALG11-like 1.15e-39 58 445 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.
223515 RfaB 9.03e-39 61 454 8 378
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
395425 Glycos_transf_1 6.15e-35 261 432 1 158
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.98e-186 57 454 49 447
1.74e-160 50 451 41 446
6.97e-118 57 450 4 401
9.94e-117 56 454 3 403
6.48e-114 57 453 23 420

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.26e-16 239 443 225 414
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]
2.63e-13 245 413 11 159
Crystal Structure of the Putative Mannosyl Transferase (wbaZ-1)from Archaeoglobus fulgidus, Northeast Structural Genomics Target GR29A. [Archaeoglobus fulgidus DSM 4304]
7.14e-11 213 453 151 384
Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSO_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418]
9.73e-11 213 440 157 372
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]
1.04e-10 213 440 177 392
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.15e-104 50 454 9 415
Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Homo sapiens OX=9606 GN=ALG2 PE=1 SV=1
4.45e-104 56 454 15 415
Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Mus musculus OX=10090 GN=Alg2 PE=1 SV=2
8.56e-103 58 450 8 420
Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Rhizomucor pusillus OX=4840 GN=ALG2 PE=1 SV=1
1.88e-91 57 452 11 441
Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=ALG2 PE=3 SV=2
4.10e-91 51 453 3 420
Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Dictyostelium discoideum OX=44689 GN=alg2 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000049 0.000010

TMHMM  Annotations      download full data without filtering help

Start End
7 29