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CAZyme Information: CDH56675.1

You are here: Home > Sequence: CDH56675.1

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 Lichtheimia corymbifera
Lineage Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
CAZyme ID CDH56675.1
CAZy Family GT2
CAZyme Description glucoamylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
458 CBTN010000039|CGC2 51786.27 5.3057
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 69 449 2e-77 0.9418282548476454

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
395586 Glyco_hydro_15 1.08e-97 52 449 1 416
Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
225922 SGA1 5.73e-22 63 452 259 604
Glucoamylase (glucan-1,4-alpha-glucosidase), GH15 family [Carbohydrate transport and metabolism].
273702 oligosac_amyl 1.80e-14 70 446 275 607
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
8.22e-313 1 458 1 479
2.83e-157 44 452 70 504
1.99e-131 42 456 169 602
1.99e-131 42 456 169 602
1.99e-131 42 456 169 602

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.44e-76 42 452 2 428
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]
1.47e-76 42 452 2 428
GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]
1.51e-76 42 452 2 428
GLUCOAMYLASE-471 COMPLEXED WITH D-GLUCO-DIHYDROACARBOSE [Aspergillus awamori]
3.08e-75 42 452 2 429
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol [Aspergillus niger]
9.70e-74 42 452 2 429
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
1.59e-130 42 456 169 602
Glucoamylase 1 OS=Rhizopus oryzae OX=64495 PE=1 SV=2
2.90e-129 43 454 34 447
Glucoamylase amyD OS=Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) OX=246409 GN=amyD PE=1 SV=1
4.56e-83 37 452 154 608
Glucoamylase OS=Blastobotrys adeninivorans OX=409370 GN=GAA PE=3 SV=1
2.81e-74 42 452 26 452
Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1
5.49e-74 42 452 26 452
Glucoamylase OS=Aspergillus usamii OX=186680 GN=glaA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.720284 0.279729

TMHMM  Annotations      help

There is no transmembrane helices in CDH56675.1.