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CAZyme Information: XP_001909162.1

You are here: Home > Sequence: XP_001909162.1

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 Podospora anserina
Lineage Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
CAZyme ID XP_001909162.1
CAZy Family GH43|CBM6
CAZyme Description Glucoamylase [Source:UniProtKB/TrEMBL;Acc:B2AZ14]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
623 68269.52 5.2488
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PanserinaSmat 10888 515849 370 10518
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 47 455 1.6e-69 0.9695290858725761
CBM20 507 597 4.7e-22 0.9333333333333333

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 9.54e-124 38 455 1 413
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 8.65e-23 508 581 9 79
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.
119437 CBM20 3.23e-18 508 583 2 74
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.
395557 CBM_20 3.43e-15 508 575 3 66
Starch binding domain.
215006 CBM_2 1.86e-13 506 575 1 67
Starch binding domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 623 1 623
0.0 1 623 1 623
0.0 1 623 1 623
1.49e-232 14 623 10 611
1.44e-231 29 623 31 616

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.98e-233 29 623 31 616
Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
3.95e-183 29 580 8 564
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
2.36e-171 29 583 3 590
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1.54e-170 29 583 2 572
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1.21e-160 29 500 3 469
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
2.56e-232 29 623 31 616
Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
5.33e-171 29 583 30 586
Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
1.31e-170 5 583 5 614
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
1.31e-170 5 583 5 614
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
3.60e-170 5 583 5 613
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.795598 0.204417

TMHMM  Annotations      help

There is no transmembrane helices in XP_001909162.1.