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CAZyme Information: ACLA_078620-t26_1-p1

You are here: Home > Sequence: ACLA_078620-t26_1-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 Aspergillus clavatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
CAZyme ID ACLA_078620-t26_1-p1
CAZy Family GT15
CAZyme Description glucan 1,4-alpha-glucosidase, putative
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
617 DS027057|CGC2 67070.49 7.2696
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AclavatusNRRL1 9428 344612 287 9141
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:94 1.14.99.55:4

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 46 465 1e-73 0.9916897506925207
CBM20 517 607 2.6e-21 0.9555555555555556

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 2.90e-132 45 464 7 415
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 6.56e-46 511 617 1 106
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557 CBM_20 7.50e-29 517 607 1 89
Starch binding domain.
215006 CBM_2 2.62e-23 517 605 1 88
Starch binding domain.
119437 CBM20 3.46e-22 519 617 2 96
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.58e-272 9 617 8 614
4.50e-222 3 617 8 627
1.72e-220 1 617 26 652
2.17e-219 1 617 35 665
2.27e-219 1 617 26 656

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.26e-272 33 617 8 592
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1.25e-212 33 604 2 583
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
2.17e-202 33 617 3 615
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1.73e-182 33 497 3 458
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1.07e-181 1 604 1 593
Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.22e-208 24 617 30 625
Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
8.81e-202 23 617 17 639
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
8.81e-202 23 617 17 639
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
1.38e-200 21 617 15 638
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
3.92e-200 21 617 15 638
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000300 0.999685 CS pos: 20-21. Pr: 0.9660

TMHMM  Annotations      help

There is no transmembrane helices in ACLA_078620-t26_1-p1.