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CAZyme Information: EJT49486.1

You are here: Home > Sequence: EJT49486.1

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 Trichosporon asahii
Lineage Basidiomycota; Tremellomycetes; ; Trichosporonaceae; Trichosporon; Trichosporon asahii
CAZyme ID EJT49486.1
CAZy Family GH43
CAZyme Description Alpha-galactosidase [Source:UniProtKB/TrEMBL;Acc:J5T701]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
400 42754.24 6.4931
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_TasahiiCBS2479 8834 1186058 523 8311
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:58 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 139 366 6.5e-77 0.9694323144104804

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 7.19e-136 34 308 1 271
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
166449 PLN02808 2.48e-111 9 388 1 382
alpha-galactosidase
177874 PLN02229 1.23e-106 26 387 55 415
alpha-galactosidase
178295 PLN02692 1.15e-99 26 382 48 401
alpha-galactosidase
374582 Melibiase_2 7.79e-79 33 308 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.12e-135 26 364 22 361
8.45e-133 10 382 4 374
3.92e-131 12 382 6 374
1.29e-129 10 382 22 395
1.29e-129 10 382 22 395

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.08e-97 27 383 2 353
Chain A, alpha-galactosidase [Oryza sativa]
2.04e-86 26 383 1 354
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
3.08e-73 26 352 92 430
Crystal structure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343]
1.13e-72 27 366 2 348
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
3.87e-69 26 353 92 431
Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343],4OGZ_B Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.56e-97 26 383 65 421
Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
1.48e-96 25 383 55 408
Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
1.55e-96 26 350 32 345
Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
1.39e-95 27 382 49 400
Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1
2.88e-88 9 354 5 337
Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000793 0.999202 CS pos: 25-26. Pr: 0.9217

TMHMM  Annotations      help

There is no transmembrane helices in EJT49486.1.