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CAZyme Information: APA13257.1

You are here: Home > Sequence: APA13257.1

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 Sclerotinia sclerotiorum
Lineage Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Sclerotinia; Sclerotinia sclerotiorum
CAZyme ID APA13257.1
CAZy Family GH72
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
616 CP017823|CGC3 67027.04 4.8540
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ssclerotiorum1980UF-70 11368 665079 238 11130
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 65 457 5.9e-70 0.9335180055401662
CBM20 507 596 1.1e-22 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 6.36e-121 42 458 2 417
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 6.70e-39 506 606 7 106
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 1.17e-23 507 601 2 95
Starch binding domain.
119437 CBM20 1.25e-19 508 606 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.
99882 CBM20_CGTase 3.08e-18 507 601 4 99
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. 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
0.0 1 616 1 616
0.0 1 616 1 615
0.0 1 616 1 615
1.48e-290 1 616 1 617
7.35e-286 5 616 7 616

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.54e-287 5 616 7 616
Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
4.71e-193 31 592 7 579
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
6.69e-189 31 592 1 583
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6.44e-183 32 606 3 615
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1.30e-163 32 489 3 458
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.31e-286 5 616 7 616
Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
6.40e-183 1 606 1 639
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
6.40e-183 1 606 1 639
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
1.29e-179 1 606 1 638
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
1.61e-178 44 606 39 609
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
0.000206 0.999736 CS pos: 19-20. Pr: 0.9825

TMHMM  Annotations      help

There is no transmembrane helices in APA13257.1.