CAZyme Information: AEO58507.1

Basic Information

• Species: Thermothelomyces thermophilus
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Thermothelomyces; Thermothelomyces thermophilus
• CAZyme ID: AEO58507.1
• CAZy Family: GH3
• CAZyme Description: glycoside hydrolase family 13 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
471		53550.71	5.3883

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TthermophilusATCC42464	9292	573729	195	9097

• Gene Location: location=CP003005:443084-444957(-)

Full Sequence      

MPALAALGVTKLWIPPACKAAAGPEGNGYDAYDLWDLGEFEQKGSRRTKWGTKEELVRMA
EAARREGVAVLFDAVLNHKMGADRRERAVATRVEDRDRRVEVEAEVEGEEKREIGAWTGF
EFPGRKGKYSGMRWSKEHFTGVDYDDLKGEKGVWKFEGKEWAEDVDEELGNYDFLLAADI
DHRHPEVRADLFRWIEWLPSQVQLGGLRLDAIKHYSFSFLRDFVAHVRQRVGQGWFIVGE
YWREDSEYLAKFIEFMDHQISLFDVQLVSNFSKVSVLEEKGDLREILDDTLALWKPENAV
TPIAPFFIPFAYAIILLRANCGLPCVFFADLFGSVRQDAQSDFASFVPPTSGGAILPKMM
LARRFWAYGSQYDYFDDPHCVGFTRVGHSSQCGGHGLAVVMTNAWEYASKRMFVGKQHAG
EIWTDLLKWCPGRIIIDEDGWGVFPVGHRSVAVWVNTRAVGREVADTFALH

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	4	333	1e-116	0.9912280701754386

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200457	AmyAc_bac_fung_AmyA	0.0	2	364	27	390	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	7.54e-176	2	455	29	479	cytoplasmic alpha-amylase; Reviewed
200453	AmyAc_arch_bac_plant_AmyA	4.50e-27	2	332	25	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.
215419	PLN02784	1.32e-13	2	258	528	712	alpha-amylase
223443	AmyA	9.84e-13	4	455	38	443	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO58507.1|GH13_5	0.0	1	471	1	471
CAP62108.1|GH13_5	1.89e-209	1	463	2	460
CDP29184.1|GH13_5	5.02e-208	1	463	95	553
VBB80949.1|GH13_5	3.10e-203	1	463	95	568
QBZ66474.1|GH13_5	1.09e-175	1	466	69	538

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	2.05e-106	4	465	33	489	Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1VJS_A	3.36e-106	4	455	32	481	Structure Of Alpha-Amylase Precursor [Bacillus licheniformis]
1OB0_A	6.70e-106	4	455	32	481	Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]
6TOY_A	1.34e-105	4	455	32	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	7.50e-105	4	455	32	481	Bacillus Licheniformis Alpha-Amylase [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P06278|AMY_BACLI	1.45e-105	4	455	61	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P06279|AMY_GEOSE	3.20e-101	4	465	67	525	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P00692|AMY_BACAM	4.12e-99	4	455	61	512	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P26612|AMY2_ECOLI	2.58e-95	7	455	34	490	Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3
sp|P19571|AMT6_BACS7	4.92e-95	8	456	71	517	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000013	0.000019

TMHMM  Annotations     

There is no transmembrane helices in AEO58507.1.