logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: PWY68357.1

You are here: Home > Sequence: PWY68357.1

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 eucalypticola
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus eucalypticola
CAZyme ID PWY68357.1
CAZy Family GH125
CAZyme Description glycoside hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
433 MSFU01000020|CGC1 47706.51 4.5611
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AeucalypticolaCBS122712 12207 1448314 274 11933
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 124 388 2.4e-63 0.9213973799126638

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 3.02e-121 27 330 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.
177874 PLN02229 1.95e-94 21 386 57 373
alpha-galactosidase
166449 PLN02808 7.61e-93 21 389 26 343
alpha-galactosidase
178295 PLN02692 3.53e-89 21 389 50 367
alpha-galactosidase
374582 Melibiase_2 9.51e-72 26 330 1 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 433 1 442
0.0 1 433 1 442
7.69e-314 1 433 1 443
7.69e-314 1 433 1 443
8.97e-313 1 433 1 443

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.61e-171 17 433 1 414
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
1.11e-85 21 389 3 320
Chain A, alpha-galactosidase [Oryza sativa]
5.01e-81 21 389 3 320
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
8.42e-79 21 389 3 344
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
1.88e-75 21 374 24 361
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.37e-314 1 433 1 443
Probable alpha-galactosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglB PE=3 SV=1
1.59e-313 1 433 1 443
Probable alpha-galactosidase B OS=Aspergillus niger OX=5061 GN=aglB PE=2 SV=1
6.55e-253 10 433 13 442
Probable alpha-galactosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglB PE=3 SV=1
6.55e-253 10 433 13 442
Probable alpha-galactosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglB PE=3 SV=1
2.64e-244 14 433 20 447
Probable alpha-galactosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aglB PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000255 0.999714 CS pos: 20-21. Pr: 0.7751

TMHMM  Annotations      help

There is no transmembrane helices in PWY68357.1.