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CAZyme Information: EAQ86714.1

You are here: Home > Sequence: EAQ86714.1

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 Chaetomium globosum
Lineage Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
CAZyme ID EAQ86714.1
CAZy Family GH11
CAZyme Description Glucoamylase [Source:UniProtKB/TrEMBL;Acc:Q2GVN7]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
606 65304.86 9.3396
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CglobosumCBS148.51 11232 306901 184 11048
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:94 3.2.1.3:94 3.2.1.1:13

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 55 228 6.5e-38 0.45706371191135736
CBM20 490 557 2.9e-19 0.7

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 1.33e-121 48 444 1 416
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 5.48e-35 484 594 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 8.65e-23 490 556 1 66
Starch binding domain.
119437 CBM20 2.69e-17 492 557 2 66
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 3.72e-16 492 556 3 67
Starch binding domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.45e-259 1 595 1 628
1.45e-254 1 595 1 657
8.30e-231 38 556 2 566
2.73e-228 1 556 1 582
2.73e-228 1 556 1 582

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.12e-195 38 555 1 562
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3.05e-153 38 556 2 581
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2.12e-143 38 506 2 470
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
7.05e-143 42 556 11 559
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1.10e-141 37 556 29 573
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
1.58e-221 1 555 1 591
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
4.73e-159 39 556 30 578
Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
2.34e-152 36 556 24 605
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
2.34e-152 36 556 24 605
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
8.26e-151 36 556 24 576
Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000408 0.999552 CS pos: 20-21. Pr: 0.9798

TMHMM  Annotations      help

There is no transmembrane helices in EAQ86714.1.