CAZyme Information: EHY59074.1

Basic Information

• Species: Exophiala dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala dermatitidis
• CAZyme ID: EHY59074.1
• CAZy Family: GT21
• CAZyme Description: amylosucrase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
635	JH226135|CGC5	72193.33	5.9883

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EdermatitidisNIHUT8656	9356	858893	71	9285

• Gene Location: location=JH226135:692244-694151(-)

Full Sequence      

MAGLCIEQQARAVKGYILQELRSRADSNSILQDKDFLARLDKHFITIYGIFAELYGRRHD
CLDQLVELIAMCGTSWLERPSELRKIDQQRELEPEWYLSNQMVGGVCYVDRYAGNLAGIK
ERIPYFRELGLTYLHLMPLFLAPEPLNDGGYAVSSYRDVRPELGSMEELRDLATALRKVG
ISLVLDLVFNHTSHEHSWAKKAAEGDAEHSNMYWIFPDRNVPTEFERTTREIFPDDHAGS
FIQLPDGRFVWSTFYHFQWDLNYSNPAVFKAMAGEMLYLANLGVDFFRMDAVAFMWKQMG
TDCENLPEVHKLLRAFNALCRVAAPSVLFKSEAIVHPDFVVQYIDRDECPLSYNPLQMAL
GWEALATRDASLLSQALERRHNIAPGCTWVNYVRSHDDIGWTFSDEDAAELGKNGAQHRK
FLNAFFVNRFPGSFARGVPFQDNPKTGDCRISGTTASLAGLESMQEYAVERILLLYSLAM
STGGVPLIYLGDEVGQLNDYSCLKDPAKMGDSRWVNRPWYPASKYVERHDPGTISGRIFT
GMRHLIQLRKATPELAGGTAVGFRTGNPTVLGYQRPGPEETLLCLCSFSDRPQWIGRDRF
LAMPVEAKDLVSGYMINLRDAGIELRPYQFLWLRC

Enzyme Prediction     

EC	2.4.1.4:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	113	498	1.5e-175	0.9975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200463	AmyAc_Amylosucrase	0.0	32	555	1	536	Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
200473	AmyAc_TreS	4.07e-64	114	495	24	374	Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
200493	AmyAc_Sucrose_phosphorylase-like_1	2.19e-54	132	553	39	440	Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
223443	AmyA	2.15e-51	114	595	26	490	Glycosidase [Carbohydrate transport and metabolism].
200481	AmyAc_Sucrose_phosphorylase-like	9.49e-49	125	553	31	437	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXJ11004.1|GH13_4	4.41e-303	1	634	1	632
BCW71100.1|GH13_4	1.73e-301	14	634	12	631
BCT74977.1|GH13_4	7.10e-300	36	634	36	638
ASN53838.1|GH13_4	9.74e-298	34	634	30	629
BCW56310.1|GH13_4	1.60e-297	33	634	30	633

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1G5A_A	2.24e-262	34	633	30	625	Amylosucrase From Neisseria Polysaccharea [Neisseria polysaccharea],1JG9_A Crystal Structure of Amylosucrase from Neisseria polysaccharea in Complex with D-glucose [Neisseria polysaccharea],1MW1_A Amylosucrase soaked with 14mM sucrose. [Neisseria polysaccharea],1MW2_A Amylosucrase soaked with 100mM sucrose [Neisseria polysaccharea],1MW3_A Amylosucrase soaked with 1M sucrose [Neisseria polysaccharea]
3UEQ_A	2.58e-262	34	633	34	629	Crystal structure of amylosucrase from Neisseria polysaccharea in complex with turanose [Neisseria polysaccharea]
1MVY_A	4.50e-262	34	633	30	625	Chain A, amylosucrase [Neisseria polysaccharea],1MW0_A Chain A, amylosucrase [Neisseria polysaccharea],1S46_A Chain A, amylosucrase [Neisseria polysaccharea],1ZS2_A Chain A, amylosucrase [Neisseria polysaccharea]
1JGI_A	5.19e-261	34	633	30	625	Chain A, amylosucrase [Neisseria polysaccharea]
4FLQ_A	1.04e-260	34	633	30	625	Crystal structure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. [Neisseria polysaccharea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9ZEU2|AMYS_NEIPO	1.33e-262	34	633	38	633	Amylosucrase OS=Neisseria polysaccharea OX=489 GN=ams PE=1 SV=1
sp|Q84HD6|AMYS_NEIME	3.08e-261	34	633	38	633	Amylosucrase OS=Neisseria meningitidis OX=487 GN=ams PE=3 SV=1
sp|P72235|TRES_PIMSR	2.86e-45	114	634	38	561	Trehalose synthase OS=Pimelobacter sp. (strain R48) OX=51662 GN=treS PE=3 SV=1
sp|P9WQ18|TRES_MYCTO	4.25e-45	113	598	65	544	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=treS PE=3 SV=1
sp|P9WQ19|TRES_MYCTU	4.25e-45	113	598	65	544	Trehalose synthase/amylase TreS OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=treS PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000072	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EHY59074.1.