CAZyme Information: EPrPRT00000016461-p1

Basic Information

• Species: Pythium arrhenomanes
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium arrhenomanes
• CAZyme ID: EPrPRT00000016461-p1
• CAZy Family: GH17
• CAZyme Description: Alpha-amylase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
526	ParrATCC12531_SC00363|CGC1	57133.06	7.9533

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ParrhenomanesATCC12531	13857	1223556	52	13805

• Gene Location: location=ParrATCC12531_SC00363:18117-19911(-)

Full Sequence      

TPSRNSSLYRSTYQDYRSLQGYAHVVYAAGRQSATVTVRTVLRVPTSTCSYSFNGASQTS
NTFTAATSLTSDLNIVVTCSSGSNTWTLALDPVNFVWQNAAVPTPSGLEGGQKGAIVDLF
GWPYADIEQDGQRNPWYFVYQPVSYRLVSRMGTRAQLRSMIQTCRANGVRVYADAVVNHM
AGGGNDVNPLHRNPSGGGCTTWGPKSSVGGSPYYSHNFAFGTNPETGLRAAAEFPAIPFG
PSDFHCERSLNAYTDPLILSAGWLEGLLDLHTGKTNVRERIAQYFVDLVGIGFSGFRIDA
IKHIGPVDTAAIFGLLNQYMGGSLPADFLMWGEVILGGEAQMLACNKDSGKLKIWSSDYP
KEMPVCGRWILPASRFVIQNDDHDQQQQGSTSRDMGDKGSVLVKNRDVGAHRNFELQLFT
RRDADWKIKVVLSSFTLFPDNTPAGFPDGYSDCAKGFDPSAGQKCTLSVPYEKAFRAGSC
GYTVEGFASVGKYTRVHRDLQIVNAMRSWTGQGSVSASQVGITGSC

Enzyme Prediction     

No EC number prediction in EPrPRT00000016461-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	132	340	1.2e-42	0.6245353159851301

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	3.83e-83	113	509	1	326	Alpha amylase catalytic domain found in bacterial and 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
200454	AmyAc_bac1_AmyA	1.11e-31	114	338	2	213	Alpha amylase catalytic domain found in bacterial 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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
214758	Aamy	2.22e-16	132	184	46	99	Alpha-amylase domain.
236518	PRK09441	2.93e-14	150	306	76	240	cytoplasmic alpha-amylase; Reviewed
200453	AmyAc_arch_bac_plant_AmyA	4.28e-09	145	195	57	113	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV88491.1|CBM21|GH13	8.55e-181	1	526	275	843
QRV73700.1|CBM21|GH13	4.83e-180	1	526	275	843
QRW02641.1|CBM21|GH13	4.83e-180	1	526	275	843
QRW16798.1|CBM21|GH13	2.04e-178	1	526	224	783
EGX42980.1|CBM21|GH13	3.13e-176	1	524	226	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1OSE_A	1.48e-30	115	387	12	303	Porcine pancreatic alpha-amylase complexed with acarbose [Sus scrofa]
1DHK_A	1.48e-30	115	387	12	303	Chain A, PORCINE PANCREATIC ALPHA-AMYLASE [Sus scrofa]
1PIF_A	2.01e-30	115	387	12	303	PIG ALPHA-AMYLASE [Sus scrofa],1PIG_A PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 [Sus scrofa],4X0N_A Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor [Sus scrofa]
1PPI_A	2.01e-30	115	387	12	303	THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION [Sus scrofa]
1KXQ_A	2.01e-30	115	387	12	303	Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_B Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_C Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_D Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_C Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_E Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_B Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P00690|AMYP_PIG	1.23e-31	88	387	5	318	Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3
sp|P00688|AMYP_MOUSE	2.99e-31	88	387	5	315	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|P00689|AMYP_RAT	2.54e-30	88	387	5	315	Pancreatic alpha-amylase OS=Rattus norvegicus OX=10116 GN=Amy2 PE=2 SV=2
sp|O97396|AMY_PHACE	1.25e-29	113	390	28	311	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P09107|AMY_TRICA	3.25e-29	113	340	26	248	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000005

TMHMM  Annotations     

There is no transmembrane helices in EPrPRT00000016461-p1.