logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: RAK71249.1

You are here: Home > Sequence: RAK71249.1

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 Aspergillus fijiensis
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fijiensis
CAZyme ID RAK71249.1
CAZy Family AA1
CAZyme Description putative alpha-1,2-mannosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
493 KZ824728|CGC1 54557.83 7.2744
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AfijiensisCBS313.89 12336 1448319 318 12018
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 253 419 2.4e-34 0.88125

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 9 451 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 1.62e-32 10 456 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.
395425 Glycos_transf_1 8.86e-26 253 437 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.
223515 RfaB 4.21e-25 10 462 4 381
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340830 GT4_sucrose_synthase 2.14e-23 176 453 134 398
sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.89e-252 10 483 5 465
3.89e-252 10 483 5 465
6.31e-250 10 485 8 472
8.95e-250 4 485 2 472
2.44e-249 10 485 45 509

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.28e-08 254 458 231 414
Crystal structure of trehalose synthase TreT from P.horikoshi [Pyrococcus horikoshii],2X6Q_B Crystal structure of trehalose synthase TreT from P.horikoshi [Pyrococcus horikoshii],2X6R_A Crystal structure of trehalose synthase TreT from P.horikoshi produced by soaking in trehalose [Pyrococcus horikoshii],2X6R_B Crystal structure of trehalose synthase TreT from P.horikoshi produced by soaking in trehalose [Pyrococcus horikoshii]
9.10e-08 366 461 267 354
UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - BH2 complex form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZER_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - BH2 complex form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZFK_A UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP-BH2 complex [Synechococcus elongatus PCC 7942 = FACHB-805]
1.20e-07 366 452 267 345
UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - apo form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZE7_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - apo form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZES_A UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP complex [Synechococcus elongatus PCC 7942 = FACHB-805],5ZES_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP complex [Synechococcus elongatus PCC 7942 = FACHB-805],5ZFK_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP-BH2 complex [Synechococcus elongatus PCC 7942 = FACHB-805]
1.82e-07 223 463 180 390
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]
1.92e-07 223 463 200 410
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
1.17e-134 11 458 13 437
Alpha-1,3/1,6-mannosyltransferase alg-2 OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alg-2 PE=3 SV=1
1.56e-102 10 463 10 440
Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=ALG2 PE=3 SV=1
4.68e-101 10 483 7 447
Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Rhizomucor pusillus OX=4840 GN=ALG2 PE=1 SV=1
2.73e-99 10 455 11 438
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
3.28e-99 10 467 18 435
Alpha-1,3/1,6-mannosyltransferase alg2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg2 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000055 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
468 490