CAZyme Information: PUG3_T011372-RA-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PUG3_T011372-RA-p1
• CAZy Family: GT71
• CAZyme Description: Alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
546		60806.53	5.6801

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GultimumBR650	14086	1223559	0	14086

• Gene Location: location=PultBR650_SC1597:3249-5560(-)

Full Sequence      

MRTDWLSMPALCLLFAVVLQALVANAQTLVKANDGTGLHVYFRTGWSAPYIHYSQGSSWT
AVPGVKMTASIDYVQFPPEEGWFRFDVAAPAAHLEFVFNNGNGVWDNNANKNYKDYRSLT
GYAHVVYAADRLSATVTARTFLRANATCTYTFNSVAQSSPTFTVTSTFTADLLIKVECTA
TANQEKWTLGLDSVNFLWQANKDIEAECQDFLGKAGYMGVKIPPPQESLFSNQWTFEDQR
NPWYITYQPYVANSYTSQRPAMEYPAVPFGPTDFHCERMTGDSRDPLYLETQWLLGLSDL
NTRKPYVRERIAQYFVDLLGIGISGLRVDAIKHIGPTDAAAIFGLLNKYLGGSFPEDFVS
WGEVVISGDADIVACNPTSSYNFYTGLDAKFLAEGISASDINKLKLWSWDYPNNFPLCGS
WILPASRFNVAKHREFEKLLFTRRDADWKIRVVLSSYTFFPDGSNGFPDGFSDCAGFDTS
LGNKCLKGVPYEKAFRAGSCGYTVENFAGGKYTRVHRDLGIVNAMRQWIGNLTEVTATDV
GITGSC

Enzyme Prediction     

EC	3.2.1.1:4	3.2.1.98:1	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.33e-60	197	528	7	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	4.64e-17	196	401	8	234	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.
367491	CBM_25	8.09e-13	35	130	3	93	Carbohydrate binding domain (family 25).
198134	CBM_25	7.02e-12	44	113	15	78	Carbohydrate binding domain.
407028	CBM53	1.73e-11	39	114	1	74	Starch/carbohydrate-binding module (family 53).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW16798.1|CBM21|GH13	6.61e-111	101	546	228	783
QRV73700.1|CBM21|GH13	2.16e-108	113	546	287	843
QRW02641.1|CBM21|GH13	2.16e-108	113	546	287	843
QRV88491.1|CBM21|GH13	8.37e-108	113	546	287	843
EGX42980.1|CBM21|GH13	3.97e-106	113	544	238	788

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VIW_A	9.33e-18	196	386	17	238	TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	1.24e-17	196	386	17	238	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]
6M4K_A	8.07e-16	203	378	29	251	Chain A, Alpha-amylase [Eisenia fetida]
6M4L_A	1.07e-15	203	355	29	226	Chain A, Alpha-amylase [Eisenia fetida],6M4M_A Chain A, Alpha-amylase [Eisenia fetida]
1OSE_A	4.11e-15	203	370	23	241	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	2.18e-19	203	386	41	256	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|P09107|AMY_TRICA	1.67e-18	196	370	33	248	Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
sp|P56634|AMY_TENMO	6.39e-17	196	386	17	238	Alpha-amylase OS=Tenebrio molitor OX=7067 PE=1 SV=1
sp|Q23835|AMY1_DROAN	2.95e-16	196	348	35	223	Alpha-amylase 1 OS=Drosophila ananassae OX=7217 GN=Amy35 PE=3 SV=3
sp|O18345|AMY2_DROAN	2.95e-16	196	348	35	223	Alpha-amylase 2 OS=Drosophila ananassae OX=7217 GN=Amy58 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000227	0.999749	CS pos: 26-27. Pr: 0.9565

TMHMM  Annotations     

Start	End
5	24