CAZyme Information: KAB8210666.1

Basic Information

• Species: Aspergillus parasiticus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus parasiticus
• CAZyme ID: KAB8210666.1
• CAZy Family: GT2
• CAZyme Description: Six-hairpin glycosidase-like protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
687		75357.11	5.8849

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AparasiticusCBS117618	14005	N/A	253	13752

• Gene Location: location=ML734941:192159-194325(+)

Full Sequence      

MAKMALGYRLPLLVSLLALFQFALAQKCWRNVTCAGPKDSAFPGLWEENIYAPSSRTVSP
KRTILSLARPNATVDYQKSKPYTLRGNGSAVVFDFGIEVGGIVTLNYTSKGGSGALGLAF
SEAKNWIGEWSDSSNGAFKGPDGALYANFTKDGSVSYVMPDESLRGGFRYLSIFLVTEDQ
VSVDVDAVSLEIGFQPTWSNLRAYQGYFHSNDDLLNRIWYSGAYTLQTNAVPVNTGRQVP
MLTKGWANNATMGPGDTILVDGAKRDRAVWPGDMGVAVPAAFVSTGDLESVKNALQTMYD
TQDKTTGAFDESGPPLSQKNSDTYHMWSMIGTYNYLLYTNDTSFLSKNWNKYQKAMDYIY
NKVDNSTGLLNVTGTRDWARWQQGYNNSEAQMILYHTLTTGARLASWAGSSSLTDKWNAQ
ATDLVQSINEYCWDDEYGAFKDNATATALHPQDANSLALLYGIVDPDRASRISKNLLQNW
TPIGAETPELPNNISPFISSFEIQGHLEIGQSARALELIRRSWGWYLNNPNGTESTVIEG
YLVDGSFGYRSDRGYSHDPSYVSHAHGWSAGPTNALTTYILGLSITSPRGLTWKIAPQFG
DLKTVEGGFTTSLGKFQASWDKSPDGYTLQFSVPPGTKGNLTLPYVRSSEKPSITIDGNN
IYKGVYYVDDTATITVSGGGRHRVVVS

Enzyme Prediction     

EC	3.2.1.174:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH78	88	643	1.2e-99	0.9861111111111112

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
407469	Bac_rhamnosid6H	2.06e-12	206	476	4	251	Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
379972	Bac_rhamnosid_C	3.49e-07	592	644	11	64	Bacterial alpha-L-rhamnosidase C-terminal domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.
283786	GDE_C	2.30e-05	270	487	31	271	Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).
183934	treF	1.52e-04	394	546	355	516	alpha,alpha-trehalase TreF.
273702	oligosac_amyl	2.48e-04	326	494	359	525	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UCK57529.1|GH78	0.0	1	687	1	686
QRD88907.1|GH78	0.0	1	687	1	686
QMW37218.1|GH78	0.0	4	687	1	674
QMW25160.1|GH78	0.0	4	687	1	674
BAE54925.1|GH78	0.0	4	687	1	619

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3CIH_A	1.17e-23	91	666	194	715	Crystal structure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

KAB8210666.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000195	0.999774	CS pos: 25-26. Pr: 0.9798

TMHMM  Annotations     

There is no transmembrane helices in KAB8210666.1.