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CAZyme Information: Z517_05527-t43_1-p1

You are here: Home > Sequence: Z517_05527-t43_1-p1

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 Fonsecaea pedrosoi
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi
CAZyme ID Z517_05527-t43_1-p1
CAZy Family GH17
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
617 67045.52 5.1015
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FpedrosoiCBS271-37 12573 1442368 46 12527
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:94

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 55 454 3.5e-74 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 9.33e-117 36 456 1 417
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 2.18e-16 512 606 9 101
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.
225922 SGA1 1.53e-12 56 452 258 598
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism].
395557 CBM_20 2.33e-11 512 603 3 91
Starch binding domain.
119437 CBM20 6.66e-11 512 606 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.66e-196 26 617 31 613
3.27e-190 26 610 31 603
4.62e-190 26 610 31 603
2.50e-187 11 611 18 605
2.50e-187 11 611 18 605

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.64e-189 11 611 18 605
Chain A, Glucoamylase P [Amorphotheca resinae],6FHW_B Chain B, Glucoamylase P [Amorphotheca resinae]
2.16e-156 21 614 2 594
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1.39e-151 25 609 1 613
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2.33e-148 26 600 1 587
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
3.02e-143 25 504 1 469
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
4.44e-188 11 611 18 605
Glucoamylase P OS=Amorphotheca resinae OX=5101 GN=GAMP PE=1 SV=1
5.34e-151 23 609 23 637
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
5.34e-151 23 609 23 637
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1
4.12e-150 23 609 23 636
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
1.84e-148 23 609 23 636
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000317 0.999678 CS pos: 23-24. Pr: 0.7302

TMHMM  Annotations      help

There is no transmembrane helices in Z517_05527-t43_1-p1.