CAZyme Information: AO090003001497-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090003001497-T-p1
• CAZy Family: AA7
• CAZyme Description: Ortholog(s) have hydrolase activity, hydrolyzing O-glycosyl compounds activity and role in carbohydrate metabolic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
539		61386.02	6.3473

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AoryzaeRIB40	12364	510516	274	12090

• Gene Location: location=Chr2_A_oryzae_RIB40:6093824-6095953(-)

Full Sequence      

MVSFFSRCFPKRRKGQQQQQQWKEIEEAARDLESRPSWNAPDNTLLLEAFEWHVPDDTCH
WRRLQHALPGLKEIGIDNIWIPPGCKAMNSSGNGYDIYDLYDLGEFDQKGSRTTKWGSRR
ELEDLVEEAKSLGVGVYWDAVLNHKAGADYPERFQAVKVDPNRRNVEISKPTEIEGWVGF
DFAGRGDQYSSMKYNWQHFNGVDWDESRRENAIFKIHAPGKDWAQDVGKDNGNYDYLMFA
NLDYSNPEVREDVLNWGTWITNELSLSGMRLDAAKHFSAGFQKEFIEHVRKTANKDLFVI
GEYWSGNLKDLLGYLQQLDHSVTAVDVPLVVNLCRTSYTKGGDLRKIFKGTLVQSKPENA
LTFVSNHDTVPGQMLENPVAQYFKPLAYALVLLRKDGHPCVFYGDLYGTLGDKPLKRACK
GKLPILTRARKLYAYGEQQDYFDQANCIGFVRYGNARHPSGMACIMSNGAAAEKRMYVGP
KHANEQWTDIMQSHESVVTIDASGYGVFPVNGMSVSVWVNSAAPDRDILHQPFDDKIYE

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	71	409	1.7e-140	0.9941520467836257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200457	AmyAc_bac_fung_AmyA	0.0	43	432	1	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.
236518	PRK09441	0.0	41	519	1	479	cytoplasmic alpha-amylase; Reviewed
200453	AmyAc_arch_bac_plant_AmyA	9.95e-39	46	407	2	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.
177990	PLN02361	1.41e-22	45	408	13	326	alpha-amylase
215419	PLN02784	9.49e-18	45	434	504	854	alpha-amylase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD83348.1|GH13_5	0.0	1	539	1	539
UDD56876.1|GH13_5	0.0	1	539	1	539
QMW28808.1|GH13_5	0.0	1	532	1	533
QMW40883.1|GH13_5	0.0	1	532	1	533
BAE58539.1|GH13_5	0.0	28	534	23	514

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1E3X_A	3.09e-161	43	519	2	481	Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A [Bacillus amyloliquefaciens],1E3Z_A Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A [Bacillus amyloliquefaciens],1E40_A Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A [Bacillus amyloliquefaciens],1E43_A Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A [Bacillus amyloliquefaciens]
1WP6_A	1.88e-160	43	520	6	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	1.88e-159	43	519	2	479	Chain A, Alpha Amylase [Sutcliffiella halmapala]
3BH4_A	2.01e-159	43	519	2	481	High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens],3BH4_B High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens]
2GJP_A	2.15e-159	43	519	6	483	Chain A, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19571|AMT6_BACS7	2.92e-159	43	520	39	517	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P00692|AMY_BACAM	2.92e-158	43	519	33	512	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P06278|AMY_BACLI	1.05e-152	43	519	33	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P06279|AMY_GEOSE	1.36e-143	40	519	36	515	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P26613|AMY2_SALTY	1.53e-122	43	519	3	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
1.000070	0.000001

TMHMM  Annotations     

There is no transmembrane helices in AO090003001497-T-p1.