CAZyme Information: PIW_T009586-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T009586-RA-p1
• CAZy Family: GH85
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
739		81957.51	6.2426

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC01959:2154-4373(-)

Full Sequence      

MSSSHFLAALFVLVQTLLMASSSKAQTLVKSNDGTGLHVYFRTGWTAPYIHYSQGSTWTT
APGVQMIKSADYVQFPAEEGWFRFDLAAPAATLEFVFNNGNGAWDNNANRNYKMTAAGTY
SVVTTVSTPPTRGACWTWEGLDQCKGSQTAFPDSDETRRWQTPPRNAVGWSAEYQDYRSL
TGYAHVVYAADRLSATVTARTFLRTNATCTYTFNSVTQSSSQFTATSSLKADLLIKVDCT
AILNGEKWTLGLDPVNFVWQANAVSQPAGMEGGQRGAVVDFFGWPYADIEAECKDFLGKA
GYMGVKIPPPQESLFSNQWTFEDQRNPWYITYQPVSYRLYSRLGSRAELRSMVQTCRANG
VRVYADAVVNHMASGGNDVYTAHRKDNGNNQCAKWSSKSSTKGSPYFTHSYAYVGNAYTG
QRPAMEYPAVPFGPTDFHCERTTGDAKDSFFMENEWLLGLSDLNTKQPYVRERIAQYFVD
LLGVGISGVRVDAIKHIDPTDAATIFGLLSKYMGGSFPADFVSWGEVVISDDKNVVACDA
SSNYNFYTGLDVKFLAEGISQADVNKLKLWSWDYPNNFPLCGSWILPPSRFVIQNDDHDQ
QPSDSVTRPMGDKGSVLVRDKDVNKHREFEKQLFTRTDADWKIRVVLSSYTFFPDGSNGF
PDGFSDCAGFDTSLGNKCLKGVPYEKAFRAGSCGYTVENFVGGKYTRVHRDLDIVNAMRG
WIGNLTQVTATDVGITESC

Enzyme Prediction     

EC	3.2.1.1:4	3.2.1.98:1	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	301	531	8.3e-45	0.6691449814126395

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.42e-98	275	721	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	4.50e-34	282	497	8	178	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	3.19e-18	286	383	18	106	Alpha-amylase domain.
367491	CBM_25	2.98e-11	34	127	3	91	Carbohydrate binding domain (family 25).
236518	PRK09441	3.81e-11	342	499	76	240	cytoplasmic alpha-amylase; Reviewed

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW16798.1|CBM21|GH13	6.20e-204	129	739	191	783
QRV88491.1|CBM21|GH13	1.46e-203	135	739	248	843
QRV73700.1|CBM21|GH13	4.11e-203	115	739	228	843
QRW02641.1|CBM21|GH13	4.11e-203	115	739	228	843
EGX42980.1|CBM21|GH13	2.01e-192	135	736	201	787

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VM5_A	6.05e-35	275	521	10	231	Recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris [Oryzias latipes]
3L2L_A	7.24e-35	275	601	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	7.24e-35	275	601	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]
1VAH_A	7.24e-35	275	601	10	302	Crystal structure of the pig pancreatic-amylase complexed with r-nitrophenyl-a-D-maltoside [Sus scrofa]
1UA3_A	7.24e-35	275	601	10	302	Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09107|AMY_TRICA	1.24e-35	275	511	26	222	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
sp|P00688|AMYP_MOUSE	1.62e-35	247	659	2	363	Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
sp|P00690|AMYP_PIG	7.55e-35	247	601	2	317	Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3
sp|P19961|AMY2B_HUMAN	1.02e-34	247	601	2	317	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1
sp|O77018|AMYR_DROTK	1.45e-34	273	652	27	349	Alpha-amylase-related protein OS=Drosophila takahashii OX=29030 GN=Amyrel PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000204	0.999785	CS pos: 25-26. Pr: 0.9619

TMHMM  Annotations     

There is no transmembrane helices in PIW_T009586-RA-p1.