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CAZyme Information: P170DRAFT_398694-t37_1-p1

You are here: Home > Sequence: P170DRAFT_398694-t37_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 steynii
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
CAZyme ID P170DRAFT_398694-t37_1-p1
CAZy Family GH131
CAZyme Description glucoamylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
638 69852.48 5.2052
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AsteyniiIBT23096 13430 1392250 235 13195
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:94 3.2.1.3:71

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 55 461 1.7e-76 0.9722991689750693
CBM20 531 615 5.9e-20 0.8666666666666667

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 9.12e-118 47 455 3 409
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 6.59e-25 522 614 1 88
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 8.77e-23 528 615 1 82
Starch binding domain.
119437 CBM20 1.74e-19 533 615 3 81
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.
215006 CBM_2 9.02e-19 530 614 1 82
Starch binding domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.18e-211 24 614 19 598
5.18e-211 24 614 19 598
5.18e-211 24 614 19 598
5.18e-211 24 614 19 598
3.09e-208 32 614 1 571

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.31e-174 36 614 8 574
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1.90e-174 36 638 3 616
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1.19e-165 36 613 2 577
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1.09e-162 36 509 3 459
Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]
1.13e-162 36 509 3 459
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.81e-196 16 638 10 612
Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
8.20e-182 48 638 39 610
Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1
2.49e-177 36 638 27 639
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
4.54e-175 36 638 27 639
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
2.13e-173 36 638 27 640
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.520782 0.479216

TMHMM  Annotations      help

There is no transmembrane helices in P170DRAFT_398694-t37_1-p1.