CAZyme Information: EGD97399.1

Basic Information

• Species: Trichophyton tonsurans
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton tonsurans
• CAZyme ID: EGD97399.1
• CAZy Family: GH55|GH55
• CAZyme Description: alpha-(1,4)-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
529		60116.76	5.6803

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TtonsuransCBS112818	8625	647933	104	8521

• Gene Location: location=GG698501:236249-238219(-)

Full Sequence      

MGQILSIYSRLRNRKWGALDEPEVAKENDLMFQGFEWHVPADQQHWNRLRESLPRLKSMG
VNNIWIPPGCKGATGGNGYDIYDLYDVGEFEQKGQTATKWGSRSDLETLISSANELDIGI
YWDAVLNHRAGADTKEKCMAVEVDPKDRTVNISEPREIEAWLGYDYPGRGTKYSELKYHW
YHFSGINYDALQQKSGIYKLVGSGNKDWAKDVSTENGNYDYLMFADVDYSNIEVTDDVKR
WIQWLGTEFKLKGLRLDAVKHYSRGFLKEFIQHIRTTVGRDWFLVAEYWTGDISDMLNYH
DQMEGLVSLFDAPLAGRFSLFAKEGQDLRRIFDKTFVQARPQKAVTFVSNHDTQPGQSLE
ILIDAWFKPLAYALILLRQDGYPCLFYGDLYGITNTESKYRLPPVDKLAALATIRTMYAY
GKQRDYFDNKKCIGFIRYGDTAHPSGLACVLNASTSAAPMSKTMYVGIRHAGEKWTEVFT
SGAATTAPVEIDPRGYGEFKIGPKSVSVWVDEGAEGRGQIDVIGEQFVD

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	56	393	2.7e-138	0.9941520467836257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200457	AmyAc_bac_fung_AmyA	0.0	28	415	1	389	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	27	510	2	479	cytoplasmic alpha-amylase; Reviewed
200453	AmyAc_arch_bac_plant_AmyA	1.74e-47	31	415	2	291	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	3.02e-20	46	395	28	360	Glycosidase [Carbohydrate transport and metabolism].
200478	AmyAc_bac_CMD_like_2	6.51e-18	51	389	49	293	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIX27107.1|GH13_5	3.10e-208	25	517	33	521
BCR86665.1|GH13_5	2.13e-203	4	521	5	529
QSS54979.1|GH13_5	3.61e-201	10	517	14	522
ABK62854.1|GH13_5	7.25e-201	10	517	14	522
QSS73251.1|GH13_5	7.25e-201	10	517	14	522

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VJS_A	1.44e-143	25	510	1	481	Structure Of Alpha-Amylase Precursor [Bacillus licheniformis]
3BH4_A	2.32e-142	28	512	2	483	High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens],3BH4_B High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens]
6TOY_A	2.63e-141	25	510	1	481	Crystal structure of Bacillus paralicheniformis wild-type alpha-amylase [Bacillus licheniformis],6TOZ_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with acarbose [Bacillus licheniformis],6TP0_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltose [Bacillus licheniformis],6TP1_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltotetraose [Bacillus licheniformis],6TP2_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with beta-cyclodextrin [Bacillus licheniformis]
1BLI_A	3.73e-141	25	510	1	481	Bacillus Licheniformis Alpha-Amylase [Bacillus licheniformis]
1OB0_A	7.46e-141	25	510	1	481	Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P06278|AMY_BACLI	6.73e-143	25	510	30	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P00692|AMY_BACAM	3.26e-141	28	512	33	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P19571|AMT6_BACS7	3.46e-136	28	512	39	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P06279|AMY_GEOSE	5.26e-132	28	510	39	515	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P26613|AMY2_SALTY	1.55e-110	27	512	2	492	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
1.000066	0.000001

TMHMM  Annotations     

There is no transmembrane helices in EGD97399.1.