CAZyme Information: AKAW_07311-t41_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: AKAW_07311-t41_1-p1
• CAZy Family: GH31
• CAZyme Description: alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
550		61159.34	4.4224

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisIFO4308	11755	1033177	267	11488

• Gene Location: location=DF126466:515498-517150(-)

Full Sequence      

MLRKFASLLGQRHMAVCLLCWCVSLATAASTEAWKTRSIYQTMTDRFALTNGSTTAPCNT
TEANYCGGSWQGTIDKLDYIQGMGFDAIMISPVIKNIAGRSKDGEAYHGYWPLDLYEINS
HFGTREELLKLSEEIHARDMYLLLDVVINNMAYMTDGEDPATTIDYNVFPQFNGSSYFHP
YCLITDWNNYTDAQWCQTGDNYTALPDLYTEHTAVQDILMDWSKSVISNYSVDGLRIDAA
KSLTPSFLPTYAETVGGFMTGEVMDSNATNVCKYQRDYLPSLPNYPLYYSMITAFLNGEP
ATLLEEIATINDLCTDTFAMVNFIEDQDVDRWAYMNDDIMLAKTALTFMMLYDGIPLVYQ
GLEQAIAYSNRAALWLTDFDTNATLYKHIAKLNAIRKHAINLDSSYINSKTYPIYQGGSE
LAFWKGTYGRQVIMVLSTAGSNGSAYTLTLPMSYGASEVVTEVLNCVNYTVNTYSQLVVD
MDKGEPRVFFPAAMMPGSGLCGYNTSNVTYSELRLAAVGSSSSSGGIHSVIPPAFASLFM
ALVAFLAFRI

Enzyme Prediction     

EC	3.2.1.1:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	67	367	1.2e-111	0.9738562091503268

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200458	AmyAc_euk_AmyA	0.0	29	401	1	374	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
200459	AmyAc_AmyMalt_CGTase_like	2.76e-66	35	397	3	388	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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.
200478	AmyAc_bac_CMD_like_2	5.52e-62	37	397	3	342	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
395077	Alpha-amylase	6.01e-43	68	364	1	326	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
370390	DUF1966	9.17e-40	413	501	1	90	Domain of unknown function (DUF1966). This domain is found in various fungal alpha-amylase proteins. Its exact function has not, as yet, been defined.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS16945.1|GH13_1	0.0	1	550	1	550
BCS05390.1|GH13_1	0.0	1	550	1	550
CAK41088.1|GH13_1|2.4.1.25	0.0	1	550	1	549
BAE58540.1|GH13_1	4.16e-237	23	531	18	536
QMW40884.1|GH13_1	4.16e-237	23	531	18	536

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2AAA_A	7.43e-133	30	502	2	476	Calcium Binding In Alpha-amylases: An X-ray Diffraction Study At 2.1 Angstroms Resolution Of Two Enzymes From Aspergillus [Aspergillus niger]
6XSJ_A	1.70e-132	26	501	19	496	Chain A, Alpha-amylase [Aspergillus oryzae],6XSJ_B Chain B, Alpha-amylase [Aspergillus oryzae],6XSV_A Chain A, Alpha-amylase [Aspergillus oryzae]
2TAA_A	3.46e-132	29	501	1	474	Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_B Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_C Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae]
6YQ7_A	6.78e-132	26	501	19	496	Taka-amylase [Aspergillus oryzae],6YQ7_B Taka-amylase [Aspergillus oryzae],6YQ9_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQ9_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae],6YQA_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQA_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae],6YQB_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQB_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae],6YQC_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQC_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae]
7P4W_A	3.67e-131	29	501	1	475	Chain A, Alpha-amylase [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q02905|AMYA_ASPAW	6.48e-137	26	501	19	496	Alpha-amylase A OS=Aspergillus awamori OX=105351 GN=amyA PE=3 SV=1
sp|Q02906|AMYB_ASPAW	6.69e-137	26	501	19	496	Alpha-amylase B OS=Aspergillus awamori OX=105351 GN=amyB PE=3 SV=1
sp|P56271|AMYA_ASPNG	3.82e-132	30	502	2	476	Acid alpha-amylase OS=Aspergillus niger OX=5061 PE=1 SV=1
sp|P0C1B4|AMYA3_ASPOR	8.73e-132	26	501	19	496	Alpha-amylase A type-3 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=amy3 PE=3 SV=1
sp|P0C1B3|AMYA1_ASPOR	3.49e-131	26	501	19	496	Alpha-amylase A type-1/2 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=amy1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000273	0.999691	CS pos: 28-29. Pr: 0.9768

TMHMM  Annotations     

Start	End
526	548