CAZyme Information: EPrPAT00000013402-p1

Basic Information

• Species: Pythium aphanidermatum
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
• CAZyme ID: EPrPAT00000013402-p1
• CAZy Family: AA1
• CAZyme Description: Alpha-amylase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
910	PaphDAOMBR444_SC0005|CGC1	97453.65	6.9597

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444	12363	1223555	58	12305

• Gene Location: location=PaphDAOMBR444_SC0005:99808-102540(+)

Full Sequence      

MGKPFAALQALLLLCAIALANAQTLVKSDDGTGIHVYFRSGWTSPYIYYNAGSGWISSPG
VKMTASSDRIRFPSESGWFKFDLAAPASSLEFVFNNGAGTWDNNANKNYKISAAGTYAVT
SSVAAPPNPVIQVKSNDGSGLHVFFRTAWQTPYIHYNKGSGWTTSPGVMLAASTDATFPV
SDGWFQVDFAAPQASLEFVFNNGAGTWENNGGNNYKVSAAGTFAFTSALTTPPYGATPSP
VPPSPTTSTPTPAPVPTTTSPVPAPTTPAPAPVPTTTAPKPTPTTTGTVTVPPVPTATPV
PSTSCQNYNGQDSCNGNNVDAPASSEERRWQTPSRNSSLYRASYQDYRSLQGYAHVVYTN
TARTSATVTVRTVLRVPSATCSYSFNGASQSSNVYTATSSLSSDLNIIVTCSSGSETWTL
KLDPVNFVWQNAAVPTPAGLEGGQKGAIVDMFGWPYADIEEECKDFLGKAGYLGVKINPP
QEAVMSDAWPQNGQRNPWYFVYQPVSYRLHSRMGTRAQLRSMIQTCRANGVRVYADAVVN
HMSGGGNDVNPLHRNPSGGSCVTWGPKSSMGGSPYYTHNFAFGVNPETGARAAAEFPAVP
YGPSDFHCERSLNAYTDGLILSAGWLEGLLDLNTGKTNVRERIAQYFVDLMGIGFSGFRI
DAMKHIGPTDTAAIFGLFNTYMGGALPADFVMWGEIILGGEAQLLACNANSGYNFYQELD
AKYAAAGLSATDIAKLKIWSSDYPKEHPACGSWILPASRFVIQNDDHDQQQQGSTSRDMQ
DKGTVLVKNRDVASHRNFEVLLFTRTDADWKIKVVLSSYTLFPDNTPAGFPDGYSDCSKG
YDSSSGQACTRSVPYEKAFRAGSCGYTVEGFTTVGKYTRVHRDLSIVNAMRSWVGLGSVS
AGQVGITGSC

Enzyme Prediction     

No EC number prediction in EPrPAT00000013402-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	471	777	3.7e-48	0.929368029739777

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	2.10e-104	445	896	1	329	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	4.05e-36	446	700	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	6.12e-22	448	546	3	99	Alpha-amylase domain.
407028	CBM53	5.43e-11	35	111	1	75	Starch/carbohydrate-binding module (family 53).
236518	PRK09441	9.29e-11	512	668	76	240	cytoplasmic alpha-amylase; Reviewed

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW16798.1|CBM21|GH13	1.72e-224	303	910	195	783
QRV88491.1|CBM21|GH13	2.45e-220	303	910	246	843
QRV73700.1|CBM21|GH13	6.93e-220	303	910	246	843
QRW02641.1|CBM21|GH13	6.93e-220	303	910	246	843
EGX42980.1|CBM21|GH13	2.21e-212	303	908	199	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VIW_A	1.30e-36	445	775	10	294	TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	2.36e-36	445	775	10	294	YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]
3DHP_A	6.27e-36	447	770	12	302	Chain A, Alpha-amylase 1 [Homo sapiens]
1PIF_A	6.27e-36	447	770	12	302	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	8.43e-36	447	770	12	302	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O97396|AMY_PHACE	4.79e-39	445	774	28	311	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P09107|AMY_TRICA	1.69e-38	445	775	26	312	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
sp|P00688|AMYP_MOUSE	4.49e-37	418	770	3	314	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|P00689|AMYP_RAT	1.47e-36	418	770	3	314	Pancreatic alpha-amylase OS=Rattus norvegicus OX=10116 GN=Amy2 PE=2 SV=2
sp|P00690|AMYP_PIG	2.07e-36	420	770	5	317	Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000215	0.999737	CS pos: 22-23. Pr: 0.9694

TMHMM  Annotations     

There is no transmembrane helices in EPrPAT00000013402-p1.