CAZyme Information: PYU1_T001346-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PYU1_T001346-p1
• CAZy Family: AA17
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
740		82331.25	6.6066

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GultimumDAOMBR144	15430	431595	140	15290

• Gene Location: location=PultDAOMBR144_SC2029:1024431-1026653(-)

Full Sequence      

MRTHWLSLHALCLLLAVVLQALIANGQTLVKANDGTGLHVYFRTGWSVPYIHYSQGSSWT
AVPGVKMTASTDYVQFPPEEGWFHFDVAAPAAYLEFVFNNGNGVWDNNANKNYKVTSAGT
YSVVTTVSTPPTRGSCWTWDGLDTCKGTQTDFPDSDETRRWQTPPRNAASWSFEYQDYRS
LTGYAHVVYAADRLSATVTARTFLRANATCTYTFNSVVQSSPTFTVTSAFTADLLIKVEC
AATANQEKWTLGLDPVNFLWQANKVVQPPGMENGQRGAVVDFFGWPYKDIEAECQDFLGK
AGYMGIKIPPPQESLFSNQWTFEDQRNPWYITYQPVSYRLYSRLGSRSELRSMIQTCRAN
GVRVYADAVVNHMASGGNDVYTAHRKNNGNNNCATWGSKSSTKGSPYFTHSYQYVANSYT
SLRPAMEYPAVPFGPTDFHCERMTGDSRDPLYLETQWLLGLSDLNTRKPYVRERIAQYFV
DLLGIGISGLRVDAIKHIGPTDAAAIFGLLNKYLGGSFPEDFVSWGEVVISGDADIVACN
PTSSYNFYTGLDAKFLAEGISASDINKLKLWSWDYPNNFPLCGSWILPASRFVIQNDDHD
QQPADSVTRPMGDKGSVLVRDKDVAKHREFEKLLFTRRDADWKIRVVLSSYTFFPDGSNG
FPDGFSDCAGFDTSLGNKCLKGVPYEKAFRAGSCGYTVENFAGGKYTRVHRDLGIVNAMR
QWIGNLTEVTATDVGITGSC

Enzyme Prediction     

EC	3.2.1.1:4	3.2.1.98:1	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	302	533	2.3e-44	0.6691449814126395

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.42e-101	276	722	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	6.05e-35	283	536	8	217	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	2.13e-18	287	390	18	112	Alpha-amylase domain.
367491	CBM_25	3.98e-12	35	128	3	91	Carbohydrate binding domain (family 25).
198134	CBM_25	2.37e-11	44	113	15	78	Carbohydrate binding domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRV73700.1|CBM21|GH13	5.33e-204	116	740	228	843
QRW02641.1|CBM21|GH13	5.33e-204	116	740	228	843
QRV88491.1|CBM21|GH13	1.20e-202	123	740	235	843
QRW16798.1|CBM21|GH13	1.64e-201	130	740	191	783
EGX42980.1|CBM21|GH13	1.30e-193	136	738	201	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VM5_A	2.73e-37	269	602	4	302	Recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris [Oryzias latipes]
1JXK_A	5.51e-37	273	607	5	307	Role of ethe mobile loop in the mehanism of human salivary amylase [Homo sapiens],1MFU_A Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant [Homo sapiens]
1PIF_A	5.93e-37	269	602	4	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]
3L2L_A	8.02e-37	269	602	4	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]
1OSE_A	8.02e-37	269	602	4	302	Porcine pancreatic alpha-amylase complexed with acarbose [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O97396|AMY_PHACE	1.69e-37	276	602	28	307	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P19961|AMY2B_HUMAN	1.13e-36	248	602	2	317	Alpha-amylase 2B OS=Homo sapiens OX=9606 GN=AMY2B PE=1 SV=1
sp|H2N0D4|AMY_ORYLA	1.55e-36	269	602	19	317	Alpha-amylase OS=Oryzias latipes OX=8090 PE=1 SV=1
sp|P91778|AMY_PECMA	1.98e-36	276	602	28	315	Alpha-amylase OS=Pecten maximus OX=6579 PE=2 SV=1
sp|P00690|AMYP_PIG	3.77e-36	248	602	2	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
0.000267	0.999703	CS pos: 26-27. Pr: 0.9326

TMHMM  Annotations     

Start	End
5	24