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CAZyme Information: Afu3g00610-T-p1

You are here: Home > Sequence: Afu3g00610-T-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 fumigatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
CAZyme ID Afu3g00610-T-p1
CAZy Family GH15
CAZyme Description Has domain(s) with predicted catalytic activity, glucan 1,4-alpha-glucosidase activity, hydrolase activity, hydrolyzing O-glycosyl compounds, starch binding activity and role in polysaccharide metabolic process
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
619 67029.03 4.8015
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AfumigatusAf293 10130 330879 290 9840
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:94 3.2.1.1:13

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 49 463 2.7e-74 0.9778393351800554
CBM20 517 606 6.8e-21 0.9444444444444444

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 6.59e-130 46 464 5 415
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 1.33e-41 511 617 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 1.76e-31 517 613 1 95
Starch binding domain.
215006 CBM_2 6.72e-25 517 605 1 88
Starch binding domain.
119437 CBM20 9.95e-22 519 607 2 88
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
4.46e-271 39 619 36 616
2.01e-215 21 618 19 616
8.11e-215 24 618 22 616
3.44e-214 34 619 70 679
5.96e-214 40 619 63 654

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.68e-272 39 618 14 593
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
5.43e-212 44 619 13 599
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
4.41e-205 34 607 4 604
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
4.03e-184 34 500 4 461
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
1.43e-182 34 617 32 606
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
5.11e-204 34 607 28 628
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
5.11e-204 34 607 28 628
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
2.57e-203 34 618 38 626
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
2.60e-201 34 607 28 627
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
1.48e-200 34 607 28 627
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000394 0.999591 CS pos: 22-23. Pr: 0.9750

TMHMM  Annotations      help

There is no transmembrane helices in Afu3g00610-T-p1.