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CAZyme Information: KEF52792.1

You are here: Home > Sequence: KEF52792.1

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 Exophiala aquamarina
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina
CAZyme ID KEF52792.1
CAZy Family AA4
CAZyme Description Glucoamylase [Source:UniProtKB/TrEMBL;Acc:A0A072NZG4]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
621 AMGV01000016|CGC1 67038.48 4.5218
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EaquamarinaCBS119918 13118 1182545 0 13118
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 56 455 5.2e-70 0.9501385041551247

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 1.59e-112 37 457 1 417
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 4.40e-23 513 610 9 103
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 9.68e-17 513 609 3 95
Starch binding domain.
119437 CBM20 1.19e-13 513 609 2 93
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.
99883 CBM20_alpha_amylase 1.72e-13 511 605 1 87
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.01e-187 2 606 1 597
8.61e-181 14 606 17 596
1.39e-179 14 606 17 596
2.03e-179 13 618 18 609
2.03e-179 13 618 18 609

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.00e-181 13 618 18 609
Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
7.71e-158 28 603 8 582
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
2.10e-150 27 599 1 581
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
2.52e-150 27 605 2 606
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6.19e-141 27 477 2 446
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.60e-180 13 618 18 609
Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
1.48e-151 7 604 7 628
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
3.95e-151 8 616 13 626
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
4.70e-150 7 604 7 628
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
4.84e-150 7 605 7 630
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
0.567321 0.432669

TMHMM  Annotations      help

There is no transmembrane helices in KEF52792.1.