CAZyme Information: PHYSODRAFT_556403-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_556403-t26_1-p1
• CAZy Family: PL3
• CAZyme Description: putative alpha amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
712		77133.55	5.6559

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

Full Sequence      

MTASTDPTYPASVGWFQYDVAVPQASLEFVFNNGNGVWDNNKNANYEATSAGKWIVMSTV
SVPPATTTTTTPTTAPAPPTATPKPTTASPTPTSTAAPSPTTSAPTPSGSCYNYNGQDSC
SSSTQTELPASDDQRKWQTPPRNASGWSTDYQDYRSLTGYAHVVYGAARTSATVTVRTFL
RVASATCSFTFNGVKSTSATYQVTNALKDDLIIVVTCTDGTDTWTLELDPVNFVWQNNAV
NQPSGMKGGQKGAIVDLFGWPYDDIAQECSDFLGKASYMGVKINPPQESVLTDAWPQNGQ
RNPWYFVYQPVSYRLYSRLGTRAQLRSMIQTCRANGVRVYADAVVNHMSGGGNDVLSHRY
SSGGSCVTWGAKSSAKHSPYYTHSYTYGVNEYTKARPALEFPAVPYGPSDFHCERTMSSW
TDPLQLETGWLTGLTDLNTEKTYVRERIAQYFVDLLGIGFSGLRLDALKHIGPVDAGAIY
GLLNTFMGGSLPDDFISWGEVILGGEASLLACNADSGYNFYKGLDAQYAANGISSTDIAK
LKIWSSDYPKEFPICGSWILPSSRFVIQNDDHDQQNDGSSSRDMGDAGSVLIKDKDVARH
RSFEVKLFSRTDADWQIKVVLSSYTWFSNGAAGFPDGYSDCSGFDSSQGQKCTASVPYEK
AFRAGSCGYTVEGFAGGKYTRVHRDLSIVNAMRSWIGLSSVTLAGLGISGSC

Enzyme Prediction     

No EC number prediction in PHYSODRAFT_556403-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	278	579	7e-47	0.9144981412639405

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	2.44e-126	251	695	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	1.39e-37	252	505	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	8.11e-21	254	352	3	99	Alpha-amylase domain.
236518	PRK09441	2.01e-10	318	473	76	240	cytoplasmic alpha-amylase; Reviewed
200458	AmyAc_euk_AmyA	2.63e-09	313	473	88	213	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW16798.1|CBM21|GH13	QRW16798.1|CBM21|GH13	3.72e-228	111	712	197	783
QRV88491.1|CBM21|GH13	QRV88491.1|CBM21|GH13	4.64e-228	111	712	248	843
QRV73700.1|CBM21|GH13	QRV73700.1|CBM21|GH13	2.99e-226	111	712	248	843
QRW02641.1|CBM21|GH13	QRW02641.1|CBM21|GH13	2.99e-226	111	712	248	843
EGX42980.1|CBM21|GH13	EGX42980.1|CBM21|GH13	4.67e-217	111	710	201	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1BVN_P	1BVN_P	1.13e-41	254	629	13	347	Pig Pancreatic Alpha-Amylase In Complex With The Proteinaceous Inhibitor Tendamistat [Sus scrofa]
1PIF_A	1PIF_A	1.53e-41	253	629	12	347	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	1PPI_A	2.09e-41	253	629	12	347	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]
1UA3_A	1UA3_A	2.84e-41	253	629	12	347	Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides [Sus scrofa]
1JFH_A	1JFH_A	2.84e-41	253	629	12	347	STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O97396|AMY_PHACE	sp|O97396|AMY_PHACE	2.16e-42	251	581	28	313	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P00688|AMYP_MOUSE	sp|P00688|AMYP_MOUSE	4.37e-42	224	630	3	363	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|P00690|AMYP_PIG	sp|P00690|AMYP_PIG	8.51e-42	226	629	5	362	Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3
sp|P09107|AMY_TRICA	sp|P09107|AMY_TRICA	8.28e-40	251	580	26	312	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
sp|P19961|AMY2B_HUMAN	sp|P19961|AMY2B_HUMAN	3.99e-39	226	630	5	366	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999807	0.000266

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_556403-t26_1-p1.