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CAZyme Information: PUG3_T001601-RA-p1

You are here: Home > Sequence: PUG3_T001601-RA-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Globisporangium ultimum
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
CAZyme ID PUG3_T001601-RA-p1
CAZy Family AA2
CAZyme Description Alpha-amylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
896 96420.59 6.9243
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

Full Sequence      Download help

Enzyme Prediction      help

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

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 460 759 4.7e-50 0.9070631970260223

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
200456 AmyAc_bac_euk_AmyA 6.30e-118 434 877 1 324
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 2.01e-39 435 688 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 1.36e-20 437 535 3 99
Alpha-amylase domain.
198134 CBM_25 1.01e-13 43 113 15 82
Carbohydrate binding domain.
367491 CBM_25 1.53e-12 34 124 3 91
Carbohydrate binding domain (family 25).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.59e-236 289 896 247 843
5.07e-236 289 896 247 843
5.07e-236 289 896 247 843
5.59e-236 285 896 192 783
1.95e-218 285 894 194 788

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.65e-42 434 812 10 347
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]
3.58e-42 434 812 10 347
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]
4.84e-42 434 812 10 347
STRUCTURE OF A PANCREATIC ALPHA-AMYLASE BOUND TO A SUBSTRATE ANALOGUE AT 2.03 ANGSTROM RESOLUTION [Sus scrofa]
6.54e-42 434 812 10 347
Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_B Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_C Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXQ_D Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_C Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXT_E Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_A Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa],1KXV_B Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase [Sus scrofa]
6.54e-42 434 812 10 347
Chain A, PORCINE PANCREATIC ALPHA-AMYLASE [Sus scrofa]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.90e-44 406 813 2 363
Pancreatic alpha-amylase OS=Mus musculus OX=10090 GN=Amy2 PE=1 SV=2
5.02e-42 406 758 2 314
Pancreatic alpha-amylase OS=Rattus norvegicus OX=10116 GN=Amy2 PE=2 SV=2
1.21e-41 434 758 26 307
Alpha-amylase (Fragment) OS=Tribolium castaneum OX=7070 PE=3 SV=2
1.76e-41 406 812 2 362
Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3
6.87e-41 434 758 28 307
Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000224 0.999754 CS pos: 25-26. Pr: 0.9727

TMHMM  Annotations      download full data without filtering help

Start End
7 29