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CAZyme Information: CDH50100.1

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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 Lichtheimia corymbifera
Lineage Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
CAZyme ID CDH50100.1
CAZy Family CE4
CAZyme Description glucoamylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
448 48561.49 4.1721
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_LcorymbiferaJMRCFSU9682 12379 1263082 97 12282
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 56 438 1.7e-66 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 1.37e-109 47 439 5 416
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
225922 SGA1 5.26e-20 45 438 249 600
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism].
273702 oligosac_amyl 1.59e-09 253 436 475 607
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
4.50e-289 1 448 1 460
4.22e-143 34 448 175 609
4.22e-143 34 448 175 609
1.19e-138 19 448 156 604
1.19e-138 19 448 156 604

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.85e-85 34 439 3 425
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]
1.90e-85 34 439 3 425
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1.96e-85 34 439 3 425
GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
1.45e-84 34 439 3 426
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
5.84e-83 34 439 3 426
Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.22e-135 19 448 156 604
Glucoamylase 1 OS=Rhizopus oryzae OX=64495 PE=1 SV=2
1.87e-135 34 448 34 451
Glucoamylase amyD OS=Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) OX=246409 GN=amyD PE=1 SV=1
5.02e-85 27 444 18 453
Glucoamylase ARB_02327-1 OS=Schizophyllum commune (strain H4-8 / FGSC 9210) OX=578458 GN=SCHCODRAFT_57589 PE=1 SV=1
8.67e-84 22 439 143 605
Glucoamylase OS=Blastobotrys adeninivorans OX=409370 GN=GAA PE=3 SV=1
9.33e-83 18 439 13 449
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000229 0.999759 CS pos: 28-29. Pr: 0.8395

TMHMM  Annotations      help

There is no transmembrane helices in CDH50100.1.