CAZyme Information: EPrPIT00000021079-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000021079-p1
• CAZy Family: GH47
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
873		96132.53	6.4984

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC0664:2623-5329(-)

Full Sequence      

MGVNSLVLSALCVVTVLFQVLLHSADAQTLVKADDGTGIHVYYRTGWTVPYTHYTTGSGW
TTSPGVKMTPSTDTTQFPPALGWFKYDIAAPATSLEFVFNNGAGTWDNNNNANYKVASAG
TWSLTSKVSTPPIAAPTPVPTPSPTPAPTPAATPAATPAVTTSAVNIRVYFRTAWAPPYI
HYNQGSGWTTSPGAKMTASSDYVQFPPEEGWFKFDIVAPATSMEFVFNNGAGTWDNNGGS
NYKISSTGTYSYVTKVSTPPARGPCWTWEGLDQCQSSSQTDFPDSDETRKWQTPPRNSVN
WSLEYQDYRSLTGYAHVVYAVDRLSATVIARTFLRANATCSYTFNNAVQSSPQFTATSAL
KADLLIKVDCTVTSTGEKWGLELDPVNFVWQANFVNQPAGMENGQRGAVVDFFGWPYKDI
EEECKDXXXXLGKAGYMGVKIPPPQESLFSNQWTFEDQRNPWYIAYQPVSYRLYSRLGSR
AELRSMIQTCRTNGVRVYADAVVNHMASGGNDIYAMHRKDNGNNQCAKWSAKSSTKGSPY
FTHSYAYIGNVYTGQRPAMEYPAVPFGPTDFHCERATGNAKDPFYMEHQWLLGLSDLNTR
RPYVRERIAQYFVDLLGVGISGLRVDAIKHIGPTDAAAIFGLLSKYMGGSFPADFVSWGE
IVISDDANVVACDLSSSYNFYTGFDAKFLAEGISQSDLNKLKLWSWDYPNNFPLCGSWIL
PASRFVIQNDDHDQQPADSVTRPMGDKGSVLVRDKDVNKHREFEKLLFTRTDADWKIRVV
LSSYTFFPDGSNGFPDGFSDCAGFDTSLGNKCLKGVPYEKAFRAGSCGYTVENFVGGKYT
RVHRDLGIVNAMRSWIGNLTAVTAADVGITGTC

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	435	646	1.5e-43	0.620817843866171

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	3.50e-93	406	855	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	1.99e-35	413	632	8	179	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	1.58e-16	417	517	18	106	Alpha-amylase domain.
407028	CBM53	4.39e-14	168	244	1	75	Starch/carbohydrate-binding module (family 53).
407028	CBM53	1.10e-12	40	116	1	75	Starch/carbohydrate-binding module (family 53).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV73700.1|CBM21|GH13	1.89e-200	251	873	233	843
QRW02641.1|CBM21|GH13	1.89e-200	251	873	233	843
QRV88491.1|CBM21|GH13	2.67e-200	251	873	233	843
QRW16798.1|CBM21|GH13	1.80e-196	259	873	191	783
EGX42980.1|CBM21|GH13	2.44e-195	260	871	194	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VAH_A	9.69e-37	397	735	1	302	Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside [Sus scrofa]
1UA3_A	9.69e-37	397	735	1	302	Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides [Sus scrofa]
3L2L_A	1.76e-36	406	735	10	302	X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Limit Dextrin and Oligosaccharide [Sus scrofa],3L2M_A X-ray Crystallographic Analysis of Pig Pancreatic Alpha-Amylase with Alpha-cyclodextrin [Sus scrofa]
1HX0_A	1.76e-36	406	735	10	302	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	3.18e-36	406	735	10	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P00690|AMYP_PIG	3.42e-36	381	735	5	317	Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3
sp|P19961|AMY2B_HUMAN	1.61e-34	378	735	2	317	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1
sp|P09107|AMY_TRICA	2.14e-34	406	645	26	222	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
sp|P00688|AMYP_MOUSE	2.79e-34	378	793	2	363	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|O97396|AMY_PHACE	3.65e-34	406	735	28	307	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000209	0.999779	CS pos: 27-28. Pr: 0.9756

TMHMM  Annotations     

There is no transmembrane helices in EPrPIT00000021079-p1.