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CAZyme Information: EPrPAT00000019976-p1

You are here: Home > Sequence: EPrPAT00000019976-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 Pythium aphanidermatum
Lineage Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
CAZyme ID EPrPAT00000019976-p1
CAZy Family GH5
CAZyme Description Glucoamylase.
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
484 51906.00 7.4934
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444 12363 1223555 58 12305
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.3:9

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH15 66 471 1.6e-61 0.9473684210526315

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 2.75e-72 50 474 1 417
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
273702 oligosac_amyl 1.03e-08 211 470 403 607
oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.
225922 SGA1 2.48e-04 42 478 244 606
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.75e-95 37 481 156 613
1.76e-86 36 476 214 658
1.89e-86 36 479 162 616
1.28e-80 71 477 132 537
2.79e-77 71 475 128 530

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.05e-66 41 479 3 432
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
7.23e-65 41 479 3 432
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
1.74e-64 41 479 3 431
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]
1.78e-64 41 479 3 431
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1.83e-64 41 479 3 431
GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.02e-95 37 481 156 613
Glucoamylase OS=Blastobotrys adeninivorans OX=409370 GN=GAA PE=3 SV=1
7.64e-74 56 476 185 598
Glucoamylase 1 OS=Rhizopus oryzae OX=64495 PE=1 SV=2
3.45e-64 39 476 28 455
Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
5.80e-64 41 479 27 456
Glucoamylase OS=Aspergillus niger OX=5061 GN=GLAA PE=1 SV=1
5.80e-64 41 479 27 456
Glucoamylase OS=Aspergillus awamori OX=105351 GN=GLAA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.986753 0.013303

TMHMM  Annotations      help

There is no transmembrane helices in EPrPAT00000019976-p1.