CAZyme Information: PHYCI_91208T0-p1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: PHYCI_91208T0-p1
• CAZy Family: GT41
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
885	PcinCBS144-22_SC0016|CGC1	95555.97	5.9974

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcinnamomiCBS144-22	26201	1048749	70	26131

• Gene Location: location=PcinCBS144-22_SC0016:462525-465182(+)

Full Sequence      

MKDTHAFVGILVTLLAGFANTIAVANAQTLAKASDGSGFHVYFRTGWTTPYIHYNSGSGW
TTSPGYAMTKSTDATNFPAALGWFRYDLPASTTSLEFVFNSGNGAWDNNGNANYKIGVAG
TWQVTSSVSSPPSAAVLTASSDGTGLHIFYQTGWSAPYIHYSTGSTWTTSPGKRMTASTD
SMYPASVGWFQYDFAAPQASLEFVFNNGNGLWDNNNNANYKATSAGKWIVMSTVSVPSTA
APTPTITVPTSITASPIPTAASPTPTSTAAPSPITSAPTPSGTCYNYNGLDSCSSSTQTE
LPATDDQRKWQTPPRNASGWSTDYQDYRSLTGYAHVVYGSGRTSATITIRTYIRVAAASC
SYTFNGVESTSASYQVTNSLKEDLIIVATCTDGTDTWKLELDPVNFVWQSNAVNQPGGMK
GGQKGAIVDLFGWPYDDIAQECSDFLGKAGYMGVKINPPQESVLTDAWPQSGQRNPWYFV
YQPVSYRLYSRLGTRAQLRSMIQTCRANGVRVYADAVVNHMSGGGNDVLSHRYSSGGSCI
TWGAKSSSKHSPYFTHSYTYGLNEYTKARPALEFPAVPYGPTDFHCERTMSSWTDPLQLE
TGWLTGLTDLNTEKTYVRERIAQYFVDLLGIGFSGLRLDALKHIGPVDAGAIFGLLNTYM
GGSLPDDFISWGEVILGGEASLLACNADSGYNFYKGLDAQYVANGISSTDIAKLKIWSSD
YPKEFPICGSWILPASRFVIQNDDHDQQNDGSSSRDMGDSGSVLIKDKDVAKHRSFEVKL
FSRTDADWQIKVVLSSYTWFANGAAGFPDGYSDCSGFDSSQGQTCTASVPYEKAFRVGSC
GYTVEGFAGGKYTRVHRDLSIVNAMRNWIGLSSVTLSDVGISGSC

Enzyme Prediction     

EC	3.2.1.1:4	3.2.1.98:1	3.2.1.1:4	3.2.1.98:1	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	450	751	5.7e-47	0.9144981412639405

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.31e-124	424	868	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	4.61e-37	425	678	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	2.39e-22	427	525	3	99	Alpha-amylase domain.
198134	CBM_25	2.47e-11	45	118	15	82	Carbohydrate binding domain.
407028	CBM53	9.29e-11	40	116	1	75	Starch/carbohydrate-binding module (family 53).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV88491.1|CBM21|GH13	1.33e-227	284	885	248	843
QRV73700.1|CBM21|GH13	2.65e-227	284	885	248	843
QRW02641.1|CBM21|GH13	2.65e-227	284	885	248	843
QRW16798.1|CBM21|GH13	1.68e-226	284	885	197	783
EGX42980.1|CBM21|GH13	6.29e-211	284	883	201	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UA3_A	1.15e-41	426	802	12	347	Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides [Sus scrofa]
1BVN_P	1.15e-41	427	802	13	347	Pig Pancreatic Alpha-Amylase In Complex With The Proteinaceous Inhibitor Tendamistat [Sus scrofa]
1HX0_A	1.15e-41	426	802	12	347	Structure of pig pancreatic alpha-amylase complexed with the 'truncate' acarbose molecule (pseudotrisaccharide) [Sus scrofa],1WO2_A Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion [Sus scrofa]
1PIF_A	1.56e-41	426	802	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	1.56e-41	426	802	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P00688|AMYP_MOUSE	2.18e-41	399	802	5	359	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|P00690|AMYP_PIG	2.29e-41	399	802	5	362	Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3
sp|O97396|AMY_PHACE	2.68e-41	424	754	28	313	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P19961|AMY2B_HUMAN	1.67e-38	399	803	5	366	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1
sp|P04746|AMYP_HUMAN	3.03e-38	399	803	5	366	Pancreatic alpha-amylase OS=Homo sapiens OX=9606 GN=AMY2A PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000253	0.999723	CS pos: 27-28. Pr: 0.9474

TMHMM  Annotations     

Start	End
7	29