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CAZyme Information: VBB76995.1

You are here: Home > Sequence: VBB76995.1

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 comata
Lineage Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata
CAZyme ID VBB76995.1
CAZy Family CE5
CAZyme Description Putative Glycoside Hydrolase Family 15
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
623 68279.65 5.3948
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PcomataTmat 13100 N/A 2652 10448
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 7e-70 0.9695290858725761
CBM20 507 597 8.3e-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 2.63e-123 38 455 1 413
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 7.05e-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 2.96e-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 3.02e-15 508 575 3 66
Starch binding domain.
215006 CBM_2 1.64e-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
4.25e-232 14 623 10 611
7.18e-232 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
2.48e-233 29 623 31 616
Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
6.38e-182 29 580 8 564
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
3.79e-170 29 583 3 590
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6.17e-170 29 583 2 572
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1.95e-159 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
1.28e-232 29 623 31 616
Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
8.55e-170 29 583 30 586
Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
2.69e-169 29 573 37 590
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
2.98e-169 5 583 5 614
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
2.98e-169 5 583 5 614
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.856981 0.143023

TMHMM  Annotations      help

There is no transmembrane helices in VBB76995.1.