CAZyme Information: EAW22346.1

Basic Information

• Species: Aspergillus fischeri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
• CAZyme ID: EAW22346.1
• CAZy Family: GH71|CBM24
• CAZyme Description: alpha-amylase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
457		52431.17	6.9322

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

• Gene Location: location=DS027688:853068-854774(-)

Full Sequence      

MDPCGNGYDVYDLYDLGEFDQKGSRATKWGTKEELLELTAAARDLGVGVHWDAVLNHKAG
ADFTERFLAVQVDPERRDVEISRPKEIEGWVGFDFNGRGDFYSSMNYRWYHFNGVDWDES
QKKNAIYKIAGPNKDWANDVGHEFGNYDYLMFANLDYSNAEVRRDLLNWGEWIGTQLPLS
GMRLDAAKHMSAAFQRDFVDHVRKTLGPDFFVISEYWRCDLKELLHFLEMMEHRVHLYDA
VLVDRFSKISRTPEADLRGILDGTLVQSKPQHAITFVMTHDTQPGQMLEVPVASFFKPLA
YALILLQNKGQPCVFWGDLYGIRGGKHPTKRSCGGRLPILTKARKLYAYGEQRDYFDERN
CIGFIRYGNRRHPSGLACIMSNAGPSQKRMFVGQQHAGEQWTDILEWHSGTVTIDRRGYG
IFPVSKVSVSVWVNARAEGRESLKSHFDTDVYKYGRS

Enzyme Prediction     

EC	3.2.1.1:2	3.2.1.116:1	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	5	322	1.1e-127	0.9298245614035088

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
236518	PRK09441	0.0	7	423	55	469	cytoplasmic alpha-amylase; Reviewed
200457	AmyAc_bac_fung_AmyA	0.0	5	346	51	391	Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. 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.
200453	AmyAc_arch_bac_plant_AmyA	1.90e-19	7	320	50	276	Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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	1.53e-15	6	423	59	433	Glycosidase [Carbohydrate transport and metabolism].
200489	AmyAc_5	1.96e-08	29	335	97	424	Alpha amylase catalytic domain found in an uncharacterized protein family. 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
BCR86665.1|GH13_5	1.99e-252	1	452	85	537
UIX27107.1|GH13_5	8.19e-245	1	454	81	534
BCS05880.1|GH13_5	7.73e-244	1	453	85	536
BCR93228.1|GH13_5	7.73e-244	1	453	85	536
QMW37842.1|GH13_5	6.42e-242	1	453	162	612

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1WP6_A	1.81e-136	7	434	57	484	Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707. [Bacillus sp. 707],1WPC_A Crystal structure of maltohexaose-producing amylase complexed with pseudo-maltononaose [Bacillus sp. 707],2D3L_A Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose. [Bacillus sp. 707],2D3N_A Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose [Bacillus sp. 707]
1W9X_A	4.51e-136	7	433	53	479	Chain A, Alpha Amylase [Sutcliffiella halmapala]
2GJP_A	5.13e-136	7	433	57	483	Chain A, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]
2DIE_A	7.57e-133	7	433	57	483	Alkaline alpha-amylase AmyK from Bacillus sp. KSM-1378 [Bacillus sp. (in: Bacteria)]
1UD2_A	4.16e-131	7	434	55	479	Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) [Bacillus sp. KSM-K38],1UD4_A Crystal structure of calcium free alpha amylase from Bacillus sp. strain KSM-K38 (AmyK38, in calcium containing solution) [Bacillus sp. KSM-K38],1UD5_A Crystal structure of AmyK38 with rubidium ion [Bacillus sp. KSM-K38],1UD6_A Crystal structure of AmyK38 with potassium ion [Bacillus sp. KSM-K38],1UD8_A Crystal structure of AmyK38 with lithium ion [Bacillus sp. KSM-K38]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19571|AMT6_BACS7	2.67e-135	7	434	90	517	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P06278|AMY_BACLI	3.79e-128	7	433	84	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P00692|AMY_BACAM	9.14e-127	1	433	78	512	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P06279|AMY_GEOSE	1.34e-126	7	433	90	515	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P26613|AMY2_SALTY	2.38e-101	7	433	55	490	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000055	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EAW22346.1.