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CAZyme Information: PAAG_02688-t30_1-p1

You are here: Home > Sequence: PAAG_02688-t30_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 Paracoccidioides lutzii
Lineage Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides lutzii
CAZyme ID PAAG_02688-t30_1-p1
CAZy Family GH13|GH13
CAZyme Description glucoamylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
648 KN293997|CGC1 70535.83 6.2548
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PlutziiPb01 8953 502779 127 8826
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:94 1.14.99.55:4

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 49 456 8.7e-77 0.9861495844875346
CBM20 529 618 4.5e-27 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 2.76e-128 45 456 3 416
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99886 CBM20_glucoamylase 2.30e-43 523 618 1 96
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 1.54e-34 529 623 1 94
Starch binding domain.
99883 CBM20_alpha_amylase 1.49e-28 529 630 1 95
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). 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 3.91e-28 531 629 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 31 630 40 646
0.0 31 630 40 646
7.38e-286 26 630 23 631
1.80e-285 31 630 83 617
7.56e-285 20 630 18 618

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.84e-241 33 630 2 616
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
2.75e-232 33 631 1 599
Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
1.49e-215 24 620 2 584
Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1.63e-213 33 498 2 467
Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]
1.69e-213 33 498 2 467
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.79e-262 46 630 39 610
Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1
8.56e-261 24 630 21 612
Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
7.03e-247 33 630 26 639
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1
3.76e-244 33 630 26 639
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
3.39e-240 33 630 26 640
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000284 0.999703 CS pos: 20-21. Pr: 0.9813

TMHMM  Annotations      help

There is no transmembrane helices in PAAG_02688-t30_1-p1.